https://proteopedia.org/api.php?action=feedcontributions&feedformat=atom&user=Matt+Routh 2026-09-22T12:07:07Z User contributions MediaWiki 1.43.8 https://proteopedia.org/index.php?title=User_talk:Eran_Hodis&diff=1012381 2009-11-01T00:03:09Z

<p>Matt Routh: </p> <hr /> <div>==News from Greece==<br /> Hi Eran,<br /> actually I was on vacation after the summer school of Erice! <br /> The last days I'm back in the lab and try to find the rythm of the experiments ;)<br /> I shown to my boss the proteopedia and my page..he is excited! Actually I'm writing a paper and I may use the proteopedia for making the pictures. I would like to ask you how can I export the pictures to my pc.<br /> We'll be in contact..you'll see the progress of my page!<br /> <br /> best wishes<br /> Maria<br /> ---------<br /> <br /> <br /> Hi Eran,<br /> Now back at home with access to my Mac. Much enjoyed meeting and talking with you. Carole and I enjoyed our round trip of Sicily, and we more or less walked our feet off in Pompei last Monday. Off to practice our golf swings now. I also talked to one of the head honchos of the Cambridge small molecule crystallographic database, and he was receptive to the idea of making a filterered subset of drugs and other biologically-active small molecules available to Proteopedia (read: ligands). If you are ever in the neighbourhood of Basel, look us up, and we can offer you a free place to sleep.<br /> best regards<br /> Trevor<br /> ---------<br /> <br /> Hi Eran. How are you? I'm Maria Ambrazi..do you remember from Erice? Can you send me your e-mail...I would like to ask you something on proteopedia!<br /> <br /> == Bad green link ==<br /> Eran,<br /> I have a green link which does not work, it should make a Ramachandran plot. When I attempt to edit it the SAT freezes and no other scenes can be loaded. In fact as I remember when I first made the scene the SAT froze. After the SAT freezes some of the links above and below this bad link no longer work. Is there a way that a developer can delete scenes?<br /> <br /> Karl<br /> <br /> ---------<br /> After I left the message for you, I decided to take a different approach and not use the link, but I would be interested in knowing what is wrong with the link if you can discover that. I named the link plot_tripep_disallowed.<br /> <br /> Karl<br /> <br /> <br /> == PDBsum site ==<br /> Eran,<br /> After exploring this site I have come to the conclusion that the entry page to this site changes from time to time. Is that correct? If so, I should give directions on the Ramachandran page how to generate the Ramachandran plot on PDBsum.<br /> <br /> By the way that site is a wonderful resource. I am going to include it in the computer resource exercise that I have my Biochemistry I students do.<br /> <br /> Karl<br /> <br /> Eran,<br /> I just realized that I was not thinking clearly this morning. I had forgotten that the url that I am using is coded for 1eve and Procheck, and therefore the site will open with the desired protein and information displayed.<br /> <br /> Karl<br /> <br /> == Proteopedia for teaching ==<br /> Hi Eran<br /> <br /> I'm in the middle of my labs using Proteopedia, and on balance I think it's a great improvement for this class - I run 6 streams of 60 students each in a 2nd year biochemistry class. Using sPDBv meant that they spent a lot of time struggling with the program, but proteopedia is letting them just think about the protein structure instead. So, overall positive. However, two things that have come up:<br /> <br /> 1) Secondary structure definitions - How does Jmol generate them? Are they user definable? Jmol is clearly using a different algorithm to sPDBv, so students are seeing inconsistency when they use both routes. (For the record, I agree with sPDBv's pick!)<br /> <br /> 2) More seriously, the display of backbone hydrogen bonds is wrong - not sure if this is something I'm doing wrong or a fault in Jmol. Backbone hydrogen bonds are being drawn between C-alphas rather than between carbonyl oxygens and peptide nitrogens. Check out the link at the very bottom of the page http://www.proteopedia.org/wiki/index.php/User:J._Shaun_Lott/BIOSCI_203 marked &quot;What is wrong with this picture?&quot; to see what I mean.<br /> <br /> cheers!<br /> <br /> Shaun<br /> <br /> == What to do with my students contributions ==<br /> <br /> Hi Eran,<br /> <br /> I am trying user talk to communicate instead of my email, since my question may be relevant to other educators. I have several student contributions that I wish to keep and others that ought to be erased eventually. I want to keep the good ones, and one bad one for illustration of a range of student abilities. I am not sure if its best to transfer the material to my page; start another page with student contributions, or to link to the student's pages. I have the passwords the student sites, so I can access the scripts. What do you suggest is best?<br /> <br /> Tom<br /> <br /> == Surfaces ==<br /> <br /> Hi Eran,<br /> <br /> I tried but could not figure out if a surface of one protomer could be colored differently from a surface of another protomer using the surface representation.<br /> <br /> Tom<br /> <br /> == more on surfaces ==<br /> <br /> Hi<br /> <br /> Surfaces are slow to load--such is life--but my experience is the same as yours. Only one color is available for the surfaces.&lt;br/&gt;<br /> my best&lt;br/&gt;<br /> Tom&lt;br/&gt;<br /> PS. So, what is the Israeli greetings/salutation during Hannukah?<br /> <br /> == Cheers Eran! ==<br /> <br /> Thanks for the info. About the template text - it even appears here when I click the + tab in your talk page. I think it should be easy enough to limit the feature by namespace, as many WP extensions seem to be ns specific. <br /> <br /> <br /> BTW, did you ever consider installing something like 'liquid threads' to make discussion more 'fully featured'? I played with it on a small wiki, and it worked OK, but when you install it you loose all old discussions. For a while I wanted to merge something like PHP BB with WP to create a forum 'channel' for each page, which should be simple enough to do... --[[User:Dan Bolser|Dan Bolser]] 10:58, 5 January 2009 (IST)<br /> <br /> == RE: ==<br /> <br /> <br /> Agreed about the template text. I'll email/message you when we have it updated. As to liquid threads, we've never considered anything like that, although its clear that the current MediaWiki system of messages is less than intuitive to say the least. We'd be hesitant to make large changes whose stability is not guaranteed, but if you think this is something we should look into, please link me to the appropriate places where I can read more about it. Eran Hodis 13:59, 5 January 2009 (IST) <br /> <br /> : With respect to 'is [this] something we should look into', I'm not really sure. It depends on how much you want Proteopedia to function as a 'community discussion forum' in addition to being a 'community education portal'. Actually, something like 'technical community discussion' was the emphasis of PDBWiki, which is why we think that it stands distinct from Proteopedia (with its emphasis on education). So basically I think its up to you to look at what is possible and assess the potential benefit, which may be marginal. Liquid threads is at http://www.mediawiki.org/wiki/Extension:LiquidThreads However, as I said, I'd be more interested in seeing a mini 'PHP BB' appearing within each talk tab http://www.phpbb.com/ I don't know why there are no efforts to implement this (that I can find). Oh... I spoke to soon ;-D http://www.mediawikiusers.com/wiki/index.php/Projects:MediaWiki/phpBB_Integration but that seems a bit thin on details TBH... Anyway, I only mentioned this because you seem to have a good capacity to work on such features, and I think that such a feature would be generally useful to the wider wiki world. All the best --[[User:Dan Bolser|Dan Bolser]] 15:24, 5 January 2009 (IST)<br /> <br /> :: After poking around I found this, http://www.mediawiki.org/wiki/Extension:AWC's_Forum which looks very promising. --[[User:Dan Bolser|Dan Bolser]] 16:00, 5 January 2009 (IST)<br /> <br /> ==RE: Models==<br /> <br /> Thanks Eran! We have been busier than expected at the CBM (but what else is new). Still, we hope to continue working on Proteopedia to upload more and more images of models we have developed - as well as some working SMART Team pages. Joel let me know that all the models made it to him intact so he should have them to show off when he gets back on your side of the world. It is a pretty neat collection of a very interesting topic - so enjoy!<br /> <br /> -Mark<br /> <br /> == Moving scenes from one page to another ==<br /> <br /> Hi Eran,<br /> <br /> I am able to copy wiki script from one page and copy it to another page using copy command: I can do ths copy &lt;nowiki&gt;&lt;scene&gt;...&lt;scene/&gt;&lt;/nowiki&gt; (assuming I wrote the syntax correctly) from User:Tom Gluick/Human Glutamine Synthetase (section) to User:Tom Gluick/Human Glutamine Synthetase (section)/quaternary a subpage. However, I would like to change the scene in the subpage, but when SAT is access in subpage, the scene is not found associated with the subpage. is there something that can be done to remedy this issue. It would certainly save me time if this were possible.<br /> <br /> Tom<br /> <br /> ==Other Media in Proteopedia?==<br /> <br /> Hi Eran,<br /> <br /> I have a question about the potential for additional media on pages. I know we can easily load and display images on Proteopedia, but is there any way to upload other file varieties - for example, simple flash animations (.swf) or something similar to that? Or, if we can't actually upload them to the Proteopedia webspace, is there any way to have files uploaded on our own server and just displayed on the proteopedia page - perhaps by using some html similar to the &lt;img src=&quot;www.filename.jpg&quot;&gt; code you can use for linking to images)?<br /> <br /> -Mark<br /> <br /> ===tilman ===<br /> Eran, you are right. That page <br /> Http://proteopedia.org/wiki/index.php/User:Tilman_Schirmer/Sandbox_10<br /> is obsolete. I've saved the content to the proper Sandbox_10.<br /> <br /> You can delete it. Thanks,<br /> Tilman<br /> ==References==<br /> <br /> Thanks for the tip Eran. I seem to stumble across cool built in features for Proteopedia like that every time I use it! Keep up the good work.<br /> <br /> -Mark<br /> <br /> == good enough? ==<br /> <br /> Would you say, [[User:Ralf Stephan/Sandbox 2|this]] is good enough to replace [[2a7g]]? What more does it need for a page 'Thermolysin'? --[[User:Ralf Stephan|Ralf Stephan]] 16:57, 7 February 2009 (IST)<br /> <br /> :It's certainly enough to replace [[2a7g]], and a great start! (please do replace it) The automatically added abstract here doesn't seem to have anything to do with the structure. Is this indeed the primary publication for the structure? Some questions/comments about your additions: Consider making &quot;metalloprotease&quot; as a interwiki link. We have a not-so-well developed page on [[Matrix_metalloproteinases]], but none on metalloproteases, so the reader may wonder what is a metalloprotease and what is its enzymatic function. It says &quot;calcium atoms (yellow)&quot; but I don't see any calcium atoms in yellow, they are green for me (as they usually are by default). It's not made entirely clear what the HEXHH motif is, could you clarify? I feel the reader would also wonder why is it important to mention in the first sentence that the protein contains zinc and several calcium atoms. Also, what is the substrate usually? The green links look just spectacular, and I'm glad to see you've quickly gotten the hang of the Scene Authoring Tools. <br /> <br /> :A page called 'Thermolysin' is a great idea, are there any other structures? We could transclude a section from your new [[2a7g]] page as well as elaborate more -- especially if there are other structures. --[[User:Eran Hodis|Eran Hodis]] 02:34, 8 February 2009 (IST)<br /> ::*There are lots of other thermolysin structures, mostly inhibitors docking and soaked with different solvent concentrations (why these?).<br /> :::Just thinking that a topic page on thermolysin could use the other structures as well to present a fuller picture.<br /> ::*So, a topic has a set of structures, ideally of all structures, with the structures pointing to 'their' nearest topic?<br /> :::That's the current mode of thinking. Of course better ideas will be adopted.<br /> ::*Regarding yellow/green, that's an example of me unconsciously giving away personal genetic data ;) Really, if I have that problem, other R/G blind people would have, too, so I'd suggest a different color for calcium.<br /> :::Hmm, yes we actually were wondering if that would be a problem when we made the scene links green -- is it a problem? Unfortunately it would be quite unfeasible to change from green scene links at this point. As far as changing calcium to a color other than green -- green might be part of a big coloring scheme that we might want to stick with. We can have a discussion on this if need be. <br /> ::*/Wrt the paper, that paper is given by PDBsum, too, one of those where the protein is just an example in a technical presentation. I should have used a different one.<br /> :::Ok, in this case then it is probably acceptable to leave out the publication abstract. If we use a more fitting abstract, but one from authors that did not solve that structure, it might send the wrong impression to readers that the wrong set of authors solved the structure. If you choose to do this, I would make it clear that the abstract is not the official one for this structure, and list the authors that did solve the structure with the appropriate reference.<br /> ::*Yes, MMPs are only a small subset of metalloproteases and should link to that WP article, too. <br /> :::Ok good.<br /> ::Thanks also for the other hints. Is there a list of all structure pages that have been enhanced manually? I know there's a manually maintained list as part of the topic page list but I think there should be something automatical such that enhancements are not lost. --[[User:Ralf Stephan|Ralf Stephan]] 10:16, 8 February 2009 (IST)<br /> :::Agreed, but the way to do this has slipped my mind at the moment. Let's see if Jaime Prilusky knows and will respond on the mailing list. --[[User:Eran Hodis|Eran Hodis]] 12:27, 8 February 2009 (IST)<br /> <br /> == java.io.File not found ==<br /> <br /> Do you understand why the applet can't find the PDB file in [[Helix-turn-helix motif]]? --[[User:Ralf Stephan|Ralf Stephan]] 17:57, 8 February 2009 (IST)<br /> :Never mind, I found it out myself: I forgot to provide a scene. --[[User:Ralf Stephan|Ralf Stephan]] 18:14, 8 February 2009 (IST)<br /> <br /> ==Image Issue==<br /> Hi Eran, <br /> I got your message and will take care of it. I think modified images were okay. <br /> Thanks!<br /> Leah<br /> <br /> ditto leah. thanks! becca<br /> <br /> ==Scrambled Eggs ==<br /> Any chance you are referring to egg cells and fertilization ? :)<br /> == Applet Behavior ==<br /> <br /> Eran, the applets in Z-DNA page seem to be behaving erratically. At times there <br /> is no display and at times they are not in the frame. There is also a problem<br /> with the sugar puckering option in DNA page. The applet freezes when this is selected.<br /> Could you please verify if you are facing the same problems?<br /> <br /> [[User:Adithya Sagar|Adithya Sagar]] 21:06, 22 October 2009 (IST)<br /> <br /> ==Image license==<br /> <br /> Originally from {Molecular cell biology. Lodish, Harvey 5 ed: - New York : W. H. Freeman and Co., 2003, 973 s. b ill. ISBN: 0-7167-4366-3. Libris: 8926100.}<br /> <br /> Original uploader was Roadnottaken at en.wikipedia 2007-03-22<br /> <br /> The image was found from Wikipedia and was a modified image that is a &quot;GNU Free Documentation License&quot;<br /> I changed the properties of my image file and it should give the proper acknowledgments.<br /> <br /> -Matt</div>

Matt Routh https://proteopedia.org/index.php?title=File:800px-Signal_transduction_v1.png&diff=1012380 2009-10-31T23:59:50Z

<p>Matt Routh: </p> <hr /> <div>Detailed overview of signal transduction pathway for apoptosis.<br /> <br /> Originally from {Molecular cell biology. Lodish, Harvey 5 ed: - New York : W. H. Freeman and Co., 2003, 973 s. b ill. ISBN: 0-7167-4366-3. Libris: 8926100.}<br /> <br /> Original uploader was Roadnottaken at en.wikipedia 2007-03-22</div>

Matt Routh https://proteopedia.org/index.php?title=MDM2&diff=1006901 2009-10-16T17:12:12Z

<p>Matt Routh: </p> <hr /> <div>{{STRUCTURE_1ycq| PDB=1ycq | SCENE= }}<br /> ===MDM2 BOUND TO HUMAN P53 Protein===<br /> <br /> ==About MDM2 Structure==<br /> The MDM2 oncoprotein is a cellular inhibitor of the p53 tumor suppressor in that it can bind the transactivation domain of p53 and downregulate its ability to activate transcription. In certain cancers, MDM2 amplification is a common event and contributes to the inactivation of p53. The crystal structure of the 109-residue amino-terminal domain of MDM2 bound to 109-residue transactivation domain peptide of p53 revealed that MDM2 has a &lt;scene name='Matt_Routh_sandbox/Hydrophobic_cavity/1'&gt;deep hydrophobic cleft&lt;/scene&gt; on which the p53 peptide binds as an amphipathic alpha helix. The interface relies on the steric complementarity between the MDM2 cleft and the hydrophobic face of the p53 alpha helix and, in particular, on a triad of p53 amino acids-Phe19, Trp23, and Leu26-which insert &lt;scene name='Matt_Routh_sandbox/Connection_to_p53/5'&gt;deep inside&lt;/scene&gt; the MDM2 cleft. These same p53 residues are also involved in transactivation, supporting the hypothesis that MDM2 inactivates p53 by concealing its transactivation domain. The structure also suggests that the amphipathic alpha helix may be a common structural motif in the binding of a diverse family of transactivation factors to the TATA-binding protein-associated factors.<br /> <br /> Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain., Kussie PH, Gorina S, Marechal V, Elenbaas B, Moreau J, Levine AJ, Pavletich NP, Science. 1996 Nov 8;274(5289):948-53. PMID:8875929<br /> <br /> From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. <br /> <br /> ==Role in Cancer== <br /> [[Image:800px-Signal transduction v1.png|Apoptosis signal pathway|400 px|thumb]]<br /> MDM2 is an active inhibitor of the p53 anti-tumorgenesis protein. When MDM2 is atached p53 is unable to release transcription factors that code for apoptosis or halting of the cell cycle. The full cell signaling pathway is very complex, but MDM2 overproduction has been shown to be connected to cancer activity.[1] Genetic amplification of MDM2 has been shown in breast, glioma, pancreaticadenocarcinoma, leucemias, Hodgkin's and nonhodgkin's lymphomas and other various cancers. [1] This broad observation outlines the importance of determining MDM2's role in tumer-genesis and how the process can be treated. <br /> <br /> ==Experimental Research==<br /> Early work in the field of MDM2 overproduction in tumor cells was done by Raphael E. Pollok et. al. This research consisted of tests done with cancerous tumor tissue and analogous tissue. DNA amplification, mRNA creation, and protein creation were all areas of interest in determining what mechanism was being utilized for the overexertion of MDM2. The amplification of the DNA would show a DNA based increase in coding for the protein. An excess of mRNA would show the increase in protein was due to increased transcription factors for MDM2. The last possibility would be that the overproduction of MDM2 was an error in translation and only protein production was to blame. <br /> <br /> These factors were tested using Southern, Northern, and Western plots to analyze DNA, mRNA, and protein production respectively. These tests use targeting antigens to test for the presence of desired proteins. The results of these tests reveled the genetic amplification of the DNA was to blame for the increased of MDM2. Also evidence that p53 protein mutations affect MDM2 were found. These results are of great use to focus treatment possibilities and further research.[1] <br /> <br /> ==Reference==<br /> 1. RAPHAEL E. POLLOCK. ''Enhanced MDM2 oncoprotein expression in soft tissue sarcoma: several possible regulatory mechanisms''.''Sarcoma''. 1997. 1,23-29.<br /> <br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:8875929&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> [[Category: Xenopus laevis]]<br /> [[Category: P53 Tumor Suppressor]]<br /> [[Category: Kussie, P H.]]<br /> [[Category: Pavletich, N P.]]<br /> [[Category: Activator]]<br /> [[Category: Anti-oncogene]]<br /> [[Category: Dna-binding]]<br /> [[Category: Nuclear protein]]<br /> [[Category: Phosphorylation]]<br /> [[Category: Transcription regulation]]</div>

Matt Routh https://proteopedia.org/index.php?title=MDM2&diff=1006899 2009-10-16T17:08:55Z

<p>Matt Routh: </p> <hr /> <div>{{STRUCTURE_1ycq| PDB=1ycq | SCENE= }}<br /> ===MDM2 BOUND TO HUMAN P53 Protein===<br /> <br /> ==About MDM2 Structure==<br /> The MDM2 oncoprotein is a cellular inhibitor of the p53 tumor suppressor in that it can bind the transactivation domain of p53 and downregulate its ability to activate transcription. In certain cancers, MDM2 amplification is a common event and contributes to the inactivation of p53. The crystal structure of the 109-residue amino-terminal domain of MDM2 bound to 109-residue transactivation domain peptide of p53 revealed that MDM2 has a &lt;scene name='Matt_Routh_sandbox/Hydrophobic_cavity/1'&gt;deep hydrophobic cleft&lt;/scene&gt; on which the p53 peptide binds as an amphipathic alpha helix. The interface relies on the steric complementarity between the MDM2 cleft and the hydrophobic face of the p53 alpha helix and, in particular, on a triad of p53 amino acids-Phe19, Trp23, and Leu26-which insert &lt;scene name='Matt_Routh_sandbox/Connection_to_p53/5'&gt;deep inside&lt;/scene&gt; the MDM2 cleft. These same p53 residues are also involved in transactivation, supporting the hypothesis that MDM2 inactivates p53 by concealing its transactivation domain. The structure also suggests that the amphipathic alpha helix may be a common structural motif in the binding of a diverse family of transactivation factors to the TATA-binding protein-associated factors.<br /> <br /> Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain., Kussie PH, Gorina S, Marechal V, Elenbaas B, Moreau J, Levine AJ, Pavletich NP, Science. 1996 Nov 8;274(5289):948-53. PMID:8875929<br /> <br /> From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. <br /> <br /> ==Role in Cancer== <br /> [[Image:800px-Signal transduction v1.png|Apoptosis signal pathway|400 px|thumb]]<br /> MDM2 is an active inhibitor of the p53 anti-tumorgenesis protein. When MDM2 is atached p53 is unable to release transcription factors that code for apoptosis or halting of the cell cycle. The full cell signaling pathway is very complex, but MDM2 overproduction has been shown to be connected to cancer activity.[1] Genetic amplification of MDM2 has been shown in breast, glioma, pancreaticadenocarcinoma, leucemias, Hodgkin's and nonhodgkin's lymphomas and other various cancers. [1] This broad observation outlines the importance of determining MDM2's role in tumer-genesis and how the process can be treated. <br /> <br /> ==Experimental Research==<br /> Early work in the field of MDM2 overproduction in tumor cells was done by Raphael E. Pollok et. al. This research consisted of tests done with cancerous tumor tissue and analogous tissue. DNA amplification, mRNA creation, and protein creation were all areas of interest in determining what mechanism was being utilized for the overexertion of MDM2. The amplification of the DNA would show a DNA based increase in coding for the protein. An excess of mRNA would show the increase in protein was due to increased transcription factors for MDM2. The last possibility would be that the overproduction of MDM2 was an error in translation and only protein production was to blame. <br /> <br /> These factors were tested using Southern, Northern, and Western plots to analyze DNA, mRNA, and protein production respectively. These tests use targeting antigens to test for the presence of desired proteins. The results of these tests reveled the genetic amplification of the DNA was to blame for the increased of MDM2. Also evidence that p53 protein mutations affect MDM2 were found. These results are of great use to focus treatment possibilities and further research.[1] <br /> <br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:8875929&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> [[Category: Xenopus laevis]]<br /> [[Category: P53 Tumor Suppressor]]<br /> [[Category: Kussie, P H.]]<br /> [[Category: Pavletich, N P.]]<br /> [[Category: Activator]]<br /> [[Category: Anti-oncogene]]<br /> [[Category: Dna-binding]]<br /> [[Category: Nuclear protein]]<br /> [[Category: Phosphorylation]]<br /> [[Category: Transcription regulation]]</div>

Matt Routh https://proteopedia.org/index.php?title=MDM2&diff=1006889 2009-10-16T15:00:26Z

<p>Matt Routh: </p> <hr /> <div>{{STRUCTURE_1ycq| PDB=1ycq | SCENE= }}<br /> ===MDM2 BOUND TO HUMAN P53 Protein===<br /> <br /> ==About MDM2 Structure==<br /> The MDM2 oncoprotein is a cellular inhibitor of the p53 tumor suppressor in that it can bind the transactivation domain of p53 and downregulate its ability to activate transcription. In certain cancers, MDM2 amplification is a common event and contributes to the inactivation of p53. The crystal structure of the 109-residue amino-terminal domain of MDM2 bound to 109-residue transactivation domain peptide of p53 revealed that MDM2 has a &lt;scene name='Matt_Routh_sandbox/Hydrophobic_cavity/1'&gt;deep hydrophobic cleft&lt;/scene&gt; on which the p53 peptide binds as an amphipathic alpha helix. The interface relies on the steric complementarity between the MDM2 cleft and the hydrophobic face of the p53 alpha helix and, in particular, on a triad of p53 amino acids-Phe19, Trp23, and Leu26-which insert &lt;scene name='Matt_Routh_sandbox/Connection_to_p53/5'&gt;deep inside&lt;/scene&gt; the MDM2 cleft. These same p53 residues are also involved in transactivation, supporting the hypothesis that MDM2 inactivates p53 by concealing its transactivation domain. The structure also suggests that the amphipathic alpha helix may be a common structural motif in the binding of a diverse family of transactivation factors to the TATA-binding protein-associated factors.<br /> <br /> Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain., Kussie PH, Gorina S, Marechal V, Elenbaas B, Moreau J, Levine AJ, Pavletich NP, Science. 1996 Nov 8;274(5289):948-53. PMID:8875929<br /> <br /> From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. <br /> <br /> ==Role in Cancer== <br /> [[Image:800px-Signal transduction v1.png|Apoptosis signal pathway|400 px|thumb]]<br /> MDM2 is an active inhibitor of the p53 anti-tumorgenesis protein. When MDM2 is atached p53 is unable to release transcription factors that code for apoptosis or halting of the cell cycle. The full cell signaling pathway is very complex, but MDM2 overproduction has been shown to be connected to cancer activity.[1] Genetic amplification of MDM2 has been shown in breast, glioma, pancreaticadenocarcinoma, leucemias, Hodgkin's and nonhodgkin's lymphomas and other various cancers. [1] This broad observation outlines the importance of determining MDM2's role in tumer-genesis and how the process can be treated. <br /> <br /> ==Experimental Research==<br /> Early work in the field of MDM2 overproduction in tumor cells was done by Raphael E. Pollok et. al. <br /> <br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:8875929&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> [[Category: Xenopus laevis]]<br /> [[Category: P53 Tumor Suppressor]]<br /> [[Category: Kussie, P H.]]<br /> [[Category: Pavletich, N P.]]<br /> [[Category: Activator]]<br /> [[Category: Anti-oncogene]]<br /> [[Category: Dna-binding]]<br /> [[Category: Nuclear protein]]<br /> [[Category: Phosphorylation]]<br /> [[Category: Transcription regulation]]</div>

Matt Routh https://proteopedia.org/index.php?title=MDM2&diff=1006888 2009-10-16T14:57:45Z

<p>Matt Routh: </p> <hr /> <div>{{STRUCTURE_1ycq| PDB=1ycq | SCENE= }}<br /> ===MDM2 BOUND TO HUMAN P53 Protein===<br /> <br /> ==About MDM2 Structure==<br /> The MDM2 oncoprotein is a cellular inhibitor of the p53 tumor suppressor in that it can bind the transactivation domain of p53 and downregulate its ability to activate transcription. In certain cancers, MDM2 amplification is a common event and contributes to the inactivation of p53. The crystal structure of the 109-residue amino-terminal domain of MDM2 bound to 109-residue transactivation domain peptide of p53 revealed that MDM2 has a &lt;scene name='Matt_Routh_sandbox/Hydrophobic_cavity/1'&gt;deep hydrophobic cleft&lt;/scene&gt; on which the p53 peptide binds as an amphipathic alpha helix. The interface relies on the steric complementarity between the MDM2 cleft and the hydrophobic face of the p53 alpha helix and, in particular, on a triad of p53 amino acids-Phe19, Trp23, and Leu26-which insert &lt;scene name='Matt_Routh_sandbox/Connection_to_p53/5'&gt;deep inside&lt;/scene&gt; the MDM2 cleft. These same p53 residues are also involved in transactivation, supporting the hypothesis that MDM2 inactivates p53 by concealing its transactivation domain. The structure also suggests that the amphipathic alpha helix may be a common structural motif in the binding of a diverse family of transactivation factors to the TATA-binding protein-associated factors.<br /> <br /> Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain., Kussie PH, Gorina S, Marechal V, Elenbaas B, Moreau J, Levine AJ, Pavletich NP, Science. 1996 Nov 8;274(5289):948-53. PMID:8875929<br /> <br /> From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. <br /> <br /> ==Role in Cancer== <br /> [[Image:800px-Signal transduction v1.png|Apoptosis signal pathway|400 px|thumb]]<br /> MDM2 is an active inhibitor of the p53 anti-tumorgenesis protein. When MDM2 is atached p53 is unable to release transcription factors that code for apoptosis or halting of the cell cycle. The full cell signaling pathway is very complex, but MDM2 overproduction has been shown to be connected to cancer activity.[1] Genetic amplification of MDM2 has been shown in breast, glioma, pancreaticadenocarcinoma, leucemias, Hodgkin's and nonhodgkin's lymphomas and other various cancers. [1] This broad observation outlines the importance of determining MDM2's role in tumer-genesis and how the process can be treated. <br /> <br /> <br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:8875929&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> [[Category: Xenopus laevis]]<br /> [[Category: P53 Tumor Suppressor]]<br /> [[Category: Kussie, P H.]]<br /> [[Category: Pavletich, N P.]]<br /> [[Category: Activator]]<br /> [[Category: Anti-oncogene]]<br /> [[Category: Dna-binding]]<br /> [[Category: Nuclear protein]]<br /> [[Category: Phosphorylation]]<br /> [[Category: Transcription regulation]]</div>

Matt Routh https://proteopedia.org/index.php?title=MDM2&diff=1006887 2009-10-16T14:56:37Z

<p>Matt Routh: </p> <hr /> <div>{{STRUCTURE_1ycq| PDB=1ycq | SCENE= }}<br /> ===MDM2 BOUND TO HUMAN P53 Protein===<br /> ==About MDM2 Structure==<br /> The MDM2 oncoprotein is a cellular inhibitor of the p53 tumor suppressor in that it can bind the transactivation domain of p53 and downregulate its ability to activate transcription. In certain cancers, MDM2 amplification is a common event and contributes to the inactivation of p53. The crystal structure of the 109-residue amino-terminal domain of MDM2 bound to 109-residue transactivation domain peptide of p53 revealed that MDM2 has a &lt;scene name='Matt_Routh_sandbox/Hydrophobic_cavity/1'&gt;deep hydrophobic cleft&lt;/scene&gt; on which the p53 peptide binds as an amphipathic alpha helix. The interface relies on the steric complementarity between the MDM2 cleft and the hydrophobic face of the p53 alpha helix and, in particular, on a triad of p53 amino acids-Phe19, Trp23, and Leu26-which insert &lt;scene name='Matt_Routh_sandbox/Connection_to_p53/5'&gt;deep inside&lt;/scene&gt; the MDM2 cleft. These same p53 residues are also involved in transactivation, supporting the hypothesis that MDM2 inactivates p53 by concealing its transactivation domain. The structure also suggests that the amphipathic alpha helix may be a common structural motif in the binding of a diverse family of transactivation factors to the TATA-binding protein-associated factors.<br /> <br /> Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain., Kussie PH, Gorina S, Marechal V, Elenbaas B, Moreau J, Levine AJ, Pavletich NP, Science. 1996 Nov 8;274(5289):948-53. PMID:8875929<br /> <br /> From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. <br /> <br /> ==Role in Cancer== <br /> [[Image:800px-Signal transduction v1.png|Apoptosis signal pathway|400 px|thumb]]<br /> MDM2 is an active inhibitor of the p53 anti-tumorgenesis protein. When MDM2 is atached p53 is unable to release transcription factors that code for apoptosis or halting of the cell cycle. The full cell signaling pathway is very complex, but MDM2 overproduction has been shown to be connected to cancer activity.[1] Genetic amplification of MDM2 has been shown in breast, glioma, pancreaticadenocarcinoma, leucemias, Hodgkin's and nonhodgkin's lymphomas and other various cancers. [1] This broad observation outlines the importance of determining MDM2's role in tumer-genesis and how the process can be treated. <br /> <br /> <br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:8875929&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> [[Category: Xenopus laevis]]<br /> [[Category: P53 Tumor Suppressor]]<br /> [[Category: Kussie, P H.]]<br /> [[Category: Pavletich, N P.]]<br /> [[Category: Activator]]<br /> [[Category: Anti-oncogene]]<br /> [[Category: Dna-binding]]<br /> [[Category: Nuclear protein]]<br /> [[Category: Phosphorylation]]<br /> [[Category: Transcription regulation]]</div>

Matt Routh https://proteopedia.org/index.php?title=MDM2&diff=1006886 2009-10-16T14:55:59Z

<p>Matt Routh: </p> <hr /> <div>{{STRUCTURE_1ycq| PDB=1ycq | SCENE= }}<br /> ===MDM2 BOUND TO HUMAN P53 Protein===<br /> ==About MDM2 Structure==<br /> The MDM2 oncoprotein is a cellular inhibitor of the p53 tumor suppressor in that it can bind the transactivation domain of p53 and downregulate its ability to activate transcription. In certain cancers, MDM2 amplification is a common event and contributes to the inactivation of p53. The crystal structure of the 109-residue amino-terminal domain of MDM2 bound to 109-residue transactivation domain peptide of p53 revealed that MDM2 has a &lt;scene name='Matt_Routh_sandbox/Hydrophobic_cavity/1'&gt;deep hydrophobic cleft&lt;/scene&gt; on which the p53 peptide binds as an amphipathic alpha helix. The interface relies on the steric complementarity between the MDM2 cleft and the hydrophobic face of the p53 alpha helix and, in particular, on a triad of p53 amino acids-Phe19, Trp23, and Leu26-which insert &lt;scene name='Matt_Routh_sandbox/Connection_to_p53/5'&gt;deep inside&lt;/scene&gt; the MDM2 cleft. These same p53 residues are also involved in transactivation, supporting the hypothesis that MDM2 inactivates p53 by concealing its transactivation domain. The structure also suggests that the amphipathic alpha helix may be a common structural motif in the binding of a diverse family of transactivation factors to the TATA-binding protein-associated factors.<br /> <br /> Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain., Kussie PH, Gorina S, Marechal V, Elenbaas B, Moreau J, Levine AJ, Pavletich NP, Science. 1996 Nov 8;274(5289):948-53. PMID:8875929<br /> <br /> From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. <br /> <br /> ==Role in Cancer== <br /> [[Image:800px-Signal transduction v1.png|Apoptosis signal pathway|500 px|thumb]]<br /> MDM2 is an active inhibitor of the p53 anti-tumorgenesis protein. When MDM2 is atached p53 is unable to release transcription factors that code for apoptosis or halting of the cell cycle. The full cell signaling pathway is very complex, but MDM2 overproduction has been shown to be connected to cancer activity.[1] Genetic amplification of MDM2 has been shown in breast, glioma, pancreaticadenocarcinoma, leucemias, Hodgkin's and nonhodgkin's lymphomas and other various cancers. [1] This broad observation outlines the importance of determining MDM2's role in tumer-genesis and how the process can be treated. <br /> <br /> <br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:8875929&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> [[Category: Xenopus laevis]]<br /> [[Category: P53 Tumor Suppressor]]<br /> [[Category: Kussie, P H.]]<br /> [[Category: Pavletich, N P.]]<br /> [[Category: Activator]]<br /> [[Category: Anti-oncogene]]<br /> [[Category: Dna-binding]]<br /> [[Category: Nuclear protein]]<br /> [[Category: Phosphorylation]]<br /> [[Category: Transcription regulation]]</div>

Matt Routh https://proteopedia.org/index.php?title=MDM2&diff=1006885 2009-10-16T14:10:58Z

<p>Matt Routh: </p> <hr /> <div>{{STRUCTURE_1ycq| PDB=1ycq | SCENE= }}<br /> ===MDM2 BOUND TO HUMAN P53 Protein===<br /> ==About MDM2 Structure==<br /> The MDM2 oncoprotein is a cellular inhibitor of the p53 tumor suppressor in that it can bind the transactivation domain of p53 and downregulate its ability to activate transcription. In certain cancers, MDM2 amplification is a common event and contributes to the inactivation of p53. The crystal structure of the 109-residue amino-terminal domain of MDM2 bound to 109-residue transactivation domain peptide of p53 revealed that MDM2 has a &lt;scene name='Matt_Routh_sandbox/Hydrophobic_cavity/1'&gt;deep hydrophobic cleft&lt;/scene&gt; on which the p53 peptide binds as an amphipathic alpha helix. The interface relies on the steric complementarity between the MDM2 cleft and the hydrophobic face of the p53 alpha helix and, in particular, on a triad of p53 amino acids-Phe19, Trp23, and Leu26-which insert &lt;scene name='Matt_Routh_sandbox/Connection_to_p53/5'&gt;deep inside&lt;/scene&gt; the MDM2 cleft. These same p53 residues are also involved in transactivation, supporting the hypothesis that MDM2 inactivates p53 by concealing its transactivation domain. The structure also suggests that the amphipathic alpha helix may be a common structural motif in the binding of a diverse family of transactivation factors to the TATA-binding protein-associated factors.<br /> <br /> Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain., Kussie PH, Gorina S, Marechal V, Elenbaas B, Moreau J, Levine AJ, Pavletich NP, Science. 1996 Nov 8;274(5289):948-53. PMID:8875929<br /> <br /> From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. <br /> <br /> ==Role in Cancer== <br /> [[Image:800px-Signal transduction v1.png|Apoptosis signal pathway|500 px|thumb]]<br /> MDM2 is an active inhibitor of the p53 anti-tumorgenesis protein. When MDM2 is atached p53 is unable to release transcription factors that code for apoptosis or halting of the cell cycle. The full cell signaling pathway is very complex, but MDM2 is usually activated by <br /> <br /> <br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:8875929&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> [[Category: Xenopus laevis]]<br /> [[Category: P53 Tumor Suppressor]]<br /> [[Category: Kussie, P H.]]<br /> [[Category: Pavletich, N P.]]<br /> [[Category: Activator]]<br /> [[Category: Anti-oncogene]]<br /> [[Category: Dna-binding]]<br /> [[Category: Nuclear protein]]<br /> [[Category: Phosphorylation]]<br /> [[Category: Transcription regulation]]</div>

Matt Routh https://proteopedia.org/index.php?title=MDM2&diff=1006884 2009-10-16T13:58:14Z

<p>Matt Routh: </p> <hr /> <div>{{STRUCTURE_1ycq| PDB=1ycq | SCENE= }}<br /> ===MDM2 BOUND TO HUMAN P53 Protein===<br /> ==About MDM2 Structure==<br /> The MDM2 oncoprotein is a cellular inhibitor of the p53 tumor suppressor in that it can bind the transactivation domain of p53 and downregulate its ability to activate transcription. In certain cancers, MDM2 amplification is a common event and contributes to the inactivation of p53. The crystal structure of the 109-residue amino-terminal domain of MDM2 bound to 109-residue transactivation domain peptide of p53 revealed that MDM2 has a &lt;scene name='Matt_Routh_sandbox/Hydrophobic_cavity/1'&gt;deep hydrophobic cleft&lt;/scene&gt; on which the p53 peptide binds as an amphipathic alpha helix. The interface relies on the steric complementarity between the MDM2 cleft and the hydrophobic face of the p53 alpha helix and, in particular, on a triad of p53 amino acids-Phe19, Trp23, and Leu26-which insert &lt;scene name='Matt_Routh_sandbox/Connection_to_p53/5'&gt;deep inside&lt;/scene&gt; the MDM2 cleft. These same p53 residues are also involved in transactivation, supporting the hypothesis that MDM2 inactivates p53 by concealing its transactivation domain. The structure also suggests that the amphipathic alpha helix may be a common structural motif in the binding of a diverse family of transactivation factors to the TATA-binding protein-associated factors.<br /> <br /> Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain., Kussie PH, Gorina S, Marechal V, Elenbaas B, Moreau J, Levine AJ, Pavletich NP, Science. 1996 Nov 8;274(5289):948-53. PMID:8875929<br /> <br /> From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. <br /> <br /> ==Role in Cancer== <br /> [[Image:800px-Signal transduction v1.png|Cell Cycle|500 px|thumb]]<br /> MDM2 is an active inhibitor of the p53 anti-tumorgenesis protein. When MDM2 is atached p53 is unable to release transcription factors that code for apoptosis or halting of the cell cycle. The full cell signaling pathway is very complex, but MDM2 is usually activated by <br /> <br /> <br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:8875929&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> [[Category: Xenopus laevis]]<br /> [[Category: P53 Tumor Suppressor]]<br /> [[Category: Kussie, P H.]]<br /> [[Category: Pavletich, N P.]]<br /> [[Category: Activator]]<br /> [[Category: Anti-oncogene]]<br /> [[Category: Dna-binding]]<br /> [[Category: Nuclear protein]]<br /> [[Category: Phosphorylation]]<br /> [[Category: Transcription regulation]]</div>

Matt Routh https://proteopedia.org/index.php?title=MDM2&diff=1006883 2009-10-16T13:57:55Z

<p>Matt Routh: </p> <hr /> <div>{{STRUCTURE_1ycq| PDB=1ycq | SCENE= }}<br /> ===MDM2 BOUND TO HUMAN P53 Protein===<br /> ==About MDM2 Structure==<br /> The MDM2 oncoprotein is a cellular inhibitor of the p53 tumor suppressor in that it can bind the transactivation domain of p53 and downregulate its ability to activate transcription. In certain cancers, MDM2 amplification is a common event and contributes to the inactivation of p53. The crystal structure of the 109-residue amino-terminal domain of MDM2 bound to 109-residue transactivation domain peptide of p53 revealed that MDM2 has a &lt;scene name='Matt_Routh_sandbox/Hydrophobic_cavity/1'&gt;deep hydrophobic cleft&lt;/scene&gt; on which the p53 peptide binds as an amphipathic alpha helix. The interface relies on the steric complementarity between the MDM2 cleft and the hydrophobic face of the p53 alpha helix and, in particular, on a triad of p53 amino acids-Phe19, Trp23, and Leu26-which insert &lt;scene name='Matt_Routh_sandbox/Connection_to_p53/5'&gt;deep inside&lt;/scene&gt; the MDM2 cleft. These same p53 residues are also involved in transactivation, supporting the hypothesis that MDM2 inactivates p53 by concealing its transactivation domain. The structure also suggests that the amphipathic alpha helix may be a common structural motif in the binding of a diverse family of transactivation factors to the TATA-binding protein-associated factors.<br /> <br /> Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain., Kussie PH, Gorina S, Marechal V, Elenbaas B, Moreau J, Levine AJ, Pavletich NP, Science. 1996 Nov 8;274(5289):948-53. PMID:8875929<br /> <br /> From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. <br /> <br /> ==Role in Cancer== <br /> [[Image:800px-Signal transduction v1.png|Cell Cycle|100 px|thumb]]<br /> MDM2 is an active inhibitor of the p53 anti-tumorgenesis protein. When MDM2 is atached p53 is unable to release transcription factors that code for apoptosis or halting of the cell cycle. The full cell signaling pathway is very complex, but MDM2 is usually activated by <br /> <br /> <br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:8875929&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> [[Category: Xenopus laevis]]<br /> [[Category: P53 Tumor Suppressor]]<br /> [[Category: Kussie, P H.]]<br /> [[Category: Pavletich, N P.]]<br /> [[Category: Activator]]<br /> [[Category: Anti-oncogene]]<br /> [[Category: Dna-binding]]<br /> [[Category: Nuclear protein]]<br /> [[Category: Phosphorylation]]<br /> [[Category: Transcription regulation]]</div>

Matt Routh https://proteopedia.org/index.php?title=MDM2&diff=1006882 2009-10-16T13:54:44Z

<p>Matt Routh: </p> <hr /> <div>{{STRUCTURE_1ycq| PDB=1ycq | SCENE= }}<br /> ===MDM2 BOUND TO HUMAN P53 Protein===<br /> ==About MDM2 Structure==<br /> The MDM2 oncoprotein is a cellular inhibitor of the p53 tumor suppressor in that it can bind the transactivation domain of p53 and downregulate its ability to activate transcription. In certain cancers, MDM2 amplification is a common event and contributes to the inactivation of p53. The crystal structure of the 109-residue amino-terminal domain of MDM2 bound to 109-residue transactivation domain peptide of p53 revealed that MDM2 has a &lt;scene name='Matt_Routh_sandbox/Hydrophobic_cavity/1'&gt;deep hydrophobic cleft&lt;/scene&gt; on which the p53 peptide binds as an amphipathic alpha helix. The interface relies on the steric complementarity between the MDM2 cleft and the hydrophobic face of the p53 alpha helix and, in particular, on a triad of p53 amino acids-Phe19, Trp23, and Leu26-which insert &lt;scene name='Matt_Routh_sandbox/Connection_to_p53/5'&gt;deep inside&lt;/scene&gt; the MDM2 cleft. These same p53 residues are also involved in transactivation, supporting the hypothesis that MDM2 inactivates p53 by concealing its transactivation domain. The structure also suggests that the amphipathic alpha helix may be a common structural motif in the binding of a diverse family of transactivation factors to the TATA-binding protein-associated factors.<br /> <br /> Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain., Kussie PH, Gorina S, Marechal V, Elenbaas B, Moreau J, Levine AJ, Pavletich NP, Science. 1996 Nov 8;274(5289):948-53. PMID:8875929<br /> <br /> From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. <br /> <br /> ==Role in Cancer== <br /> [[Image:800px-Signal transduction v1.png|50|right]]<br /> MDM2 is an active inhibitor of the p53 anti-tumorgenesis protein. When MDM2 is atached p53 is unable to release transcription factors that code for apoptosis or halting of the cell cycle. The full cell signaling pathway is very complex, but MDM2 is usually activated by <br /> <br /> <br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:8875929&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> [[Category: Xenopus laevis]]<br /> [[Category: P53 Tumor Suppressor]]<br /> [[Category: Kussie, P H.]]<br /> [[Category: Pavletich, N P.]]<br /> [[Category: Activator]]<br /> [[Category: Anti-oncogene]]<br /> [[Category: Dna-binding]]<br /> [[Category: Nuclear protein]]<br /> [[Category: Phosphorylation]]<br /> [[Category: Transcription regulation]]</div>

Matt Routh https://proteopedia.org/index.php?title=MDM2&diff=1006881 2009-10-16T13:54:20Z

<p>Matt Routh: </p> <hr /> <div>{{STRUCTURE_1ycq| PDB=1ycq | SCENE= }}<br /> ===MDM2 BOUND TO HUMAN P53 Protein===<br /> ==About MDM2 Structure==<br /> The MDM2 oncoprotein is a cellular inhibitor of the p53 tumor suppressor in that it can bind the transactivation domain of p53 and downregulate its ability to activate transcription. In certain cancers, MDM2 amplification is a common event and contributes to the inactivation of p53. The crystal structure of the 109-residue amino-terminal domain of MDM2 bound to 109-residue transactivation domain peptide of p53 revealed that MDM2 has a &lt;scene name='Matt_Routh_sandbox/Hydrophobic_cavity/1'&gt;deep hydrophobic cleft&lt;/scene&gt; on which the p53 peptide binds as an amphipathic alpha helix. The interface relies on the steric complementarity between the MDM2 cleft and the hydrophobic face of the p53 alpha helix and, in particular, on a triad of p53 amino acids-Phe19, Trp23, and Leu26-which insert &lt;scene name='Matt_Routh_sandbox/Connection_to_p53/5'&gt;deep inside&lt;/scene&gt; the MDM2 cleft. These same p53 residues are also involved in transactivation, supporting the hypothesis that MDM2 inactivates p53 by concealing its transactivation domain. The structure also suggests that the amphipathic alpha helix may be a common structural motif in the binding of a diverse family of transactivation factors to the TATA-binding protein-associated factors.<br /> <br /> Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain., Kussie PH, Gorina S, Marechal V, Elenbaas B, Moreau J, Levine AJ, Pavletich NP, Science. 1996 Nov 8;274(5289):948-53. PMID:8875929<br /> <br /> From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. <br /> <br /> ==Role in Cancer== <br /> [[Image:800px-Signal transduction v1.png|100|right]]<br /> MDM2 is an active inhibitor of the p53 anti-tumorgenesis protein. When MDM2 is atached p53 is unable to release transcription factors that code for apoptosis or halting of the cell cycle. The full cell signaling pathway is very complex, but MDM2 is usually activated by <br /> <br /> <br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:8875929&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> [[Category: Xenopus laevis]]<br /> [[Category: P53 Tumor Suppressor]]<br /> [[Category: Kussie, P H.]]<br /> [[Category: Pavletich, N P.]]<br /> [[Category: Activator]]<br /> [[Category: Anti-oncogene]]<br /> [[Category: Dna-binding]]<br /> [[Category: Nuclear protein]]<br /> [[Category: Phosphorylation]]<br /> [[Category: Transcription regulation]]</div>

Matt Routh https://proteopedia.org/index.php?title=MDM2&diff=1006880 2009-10-16T13:54:00Z

<p>Matt Routh: </p> <hr /> <div>{{STRUCTURE_1ycq| PDB=1ycq | SCENE= }}<br /> ===MDM2 BOUND TO HUMAN P53 Protein===<br /> ==About MDM2 Structure==<br /> The MDM2 oncoprotein is a cellular inhibitor of the p53 tumor suppressor in that it can bind the transactivation domain of p53 and downregulate its ability to activate transcription. In certain cancers, MDM2 amplification is a common event and contributes to the inactivation of p53. The crystal structure of the 109-residue amino-terminal domain of MDM2 bound to 109-residue transactivation domain peptide of p53 revealed that MDM2 has a &lt;scene name='Matt_Routh_sandbox/Hydrophobic_cavity/1'&gt;deep hydrophobic cleft&lt;/scene&gt; on which the p53 peptide binds as an amphipathic alpha helix. The interface relies on the steric complementarity between the MDM2 cleft and the hydrophobic face of the p53 alpha helix and, in particular, on a triad of p53 amino acids-Phe19, Trp23, and Leu26-which insert &lt;scene name='Matt_Routh_sandbox/Connection_to_p53/5'&gt;deep inside&lt;/scene&gt; the MDM2 cleft. These same p53 residues are also involved in transactivation, supporting the hypothesis that MDM2 inactivates p53 by concealing its transactivation domain. The structure also suggests that the amphipathic alpha helix may be a common structural motif in the binding of a diverse family of transactivation factors to the TATA-binding protein-associated factors.<br /> <br /> Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain., Kussie PH, Gorina S, Marechal V, Elenbaas B, Moreau J, Levine AJ, Pavletich NP, Science. 1996 Nov 8;274(5289):948-53. PMID:8875929<br /> <br /> From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. <br /> <br /> ==Role in Cancer== [[Image:800px-Signal transduction v1.png|100|right]]<br /> MDM2 is an active inhibitor of the p53 anti-tumorgenesis protein. When MDM2 is atached p53 is unable to release transcription factors that code for apoptosis or halting of the cell cycle. The full cell signaling pathway is very complex, but MDM2 is usually activated by <br /> <br /> <br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:8875929&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> [[Category: Xenopus laevis]]<br /> [[Category: P53 Tumor Suppressor]]<br /> [[Category: Kussie, P H.]]<br /> [[Category: Pavletich, N P.]]<br /> [[Category: Activator]]<br /> [[Category: Anti-oncogene]]<br /> [[Category: Dna-binding]]<br /> [[Category: Nuclear protein]]<br /> [[Category: Phosphorylation]]<br /> [[Category: Transcription regulation]]</div>

Matt Routh https://proteopedia.org/index.php?title=MDM2&diff=1006879 2009-10-16T13:53:17Z

<p>Matt Routh: </p> <hr /> <div>{{STRUCTURE_1ycq| PDB=1ycq | SCENE= }}<br /> ===MDM2 BOUND TO HUMAN P53 Protein===<br /> ==About MDM2 Structure==<br /> The MDM2 oncoprotein is a cellular inhibitor of the p53 tumor suppressor in that it can bind the transactivation domain of p53 and downregulate its ability to activate transcription. In certain cancers, MDM2 amplification is a common event and contributes to the inactivation of p53. The crystal structure of the 109-residue amino-terminal domain of MDM2 bound to 109-residue transactivation domain peptide of p53 revealed that MDM2 has a &lt;scene name='Matt_Routh_sandbox/Hydrophobic_cavity/1'&gt;deep hydrophobic cleft&lt;/scene&gt; on which the p53 peptide binds as an amphipathic alpha helix. The interface relies on the steric complementarity between the MDM2 cleft and the hydrophobic face of the p53 alpha helix and, in particular, on a triad of p53 amino acids-Phe19, Trp23, and Leu26-which insert &lt;scene name='Matt_Routh_sandbox/Connection_to_p53/5'&gt;deep inside&lt;/scene&gt; the MDM2 cleft. These same p53 residues are also involved in transactivation, supporting the hypothesis that MDM2 inactivates p53 by concealing its transactivation domain. The structure also suggests that the amphipathic alpha helix may be a common structural motif in the binding of a diverse family of transactivation factors to the TATA-binding protein-associated factors.<br /> <br /> Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain., Kussie PH, Gorina S, Marechal V, Elenbaas B, Moreau J, Levine AJ, Pavletich NP, Science. 1996 Nov 8;274(5289):948-53. PMID:8875929<br /> <br /> From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. <br /> <br /> ==Role in Cancer==<br /> MDM2 is an active inhibitor of the p53 anti-tumorgenesis protein. When MDM2 is atached p53 is unable to release transcription factors that code for apoptosis or halting of the cell cycle. The full cell signaling pathway is very complex, but MDM2 is usually activated by <br /> <br /> [[Image:800px-Signal transduction v1.png|400|right]]<br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:8875929&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> [[Category: Xenopus laevis]]<br /> [[Category: P53 Tumor Suppressor]]<br /> [[Category: Kussie, P H.]]<br /> [[Category: Pavletich, N P.]]<br /> [[Category: Activator]]<br /> [[Category: Anti-oncogene]]<br /> [[Category: Dna-binding]]<br /> [[Category: Nuclear protein]]<br /> [[Category: Phosphorylation]]<br /> [[Category: Transcription regulation]]</div>

Matt Routh https://proteopedia.org/index.php?title=MDM2&diff=1006878 2009-10-16T13:51:48Z

<p>Matt Routh: </p> <hr /> <div>{{STRUCTURE_1ycq| PDB=1ycq | SCENE= }}<br /> ===MDM2 BOUND TO HUMAN P53 Protein===<br /> ==About MDM2 Structure==<br /> The MDM2 oncoprotein is a cellular inhibitor of the p53 tumor suppressor in that it can bind the transactivation domain of p53 and downregulate its ability to activate transcription. In certain cancers, MDM2 amplification is a common event and contributes to the inactivation of p53. The crystal structure of the 109-residue amino-terminal domain of MDM2 bound to 109-residue transactivation domain peptide of p53 revealed that MDM2 has a &lt;scene name='Matt_Routh_sandbox/Hydrophobic_cavity/1'&gt;deep hydrophobic cleft&lt;/scene&gt; on which the p53 peptide binds as an amphipathic alpha helix. The interface relies on the steric complementarity between the MDM2 cleft and the hydrophobic face of the p53 alpha helix and, in particular, on a triad of p53 amino acids-Phe19, Trp23, and Leu26-which insert &lt;scene name='Matt_Routh_sandbox/Connection_to_p53/5'&gt;deep inside&lt;/scene&gt; the MDM2 cleft. These same p53 residues are also involved in transactivation, supporting the hypothesis that MDM2 inactivates p53 by concealing its transactivation domain. The structure also suggests that the amphipathic alpha helix may be a common structural motif in the binding of a diverse family of transactivation factors to the TATA-binding protein-associated factors.<br /> <br /> Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain., Kussie PH, Gorina S, Marechal V, Elenbaas B, Moreau J, Levine AJ, Pavletich NP, Science. 1996 Nov 8;274(5289):948-53. PMID:8875929<br /> <br /> From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. <br /> <br /> ==Role in Cancer==<br /> MDM2 is an active inhibitor of the p53 anti-tumorgenesis protein. When MDM2 is atached p53 is unable to release transcription factors that code for apoptosis or halting of the cell cycle. The full cell signaling pathway is very complex, but MDM2 is usually activated by <br /> <br /> [[Image:400px-Signal transduction v1.png]]<br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:8875929&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> [[Category: Xenopus laevis]]<br /> [[Category: P53 Tumor Suppressor]]<br /> [[Category: Kussie, P H.]]<br /> [[Category: Pavletich, N P.]]<br /> [[Category: Activator]]<br /> [[Category: Anti-oncogene]]<br /> [[Category: Dna-binding]]<br /> [[Category: Nuclear protein]]<br /> [[Category: Phosphorylation]]<br /> [[Category: Transcription regulation]]</div>

Matt Routh https://proteopedia.org/index.php?title=MDM2&diff=1003161 2009-10-02T00:55:41Z

<p>Matt Routh: </p> <hr /> <div>{{STRUCTURE_1ycq| PDB=1ycq | SCENE= }}<br /> ===MDM2 BOUND TO HUMAN P53 Protein===<br /> ==About MDM2 Structure==<br /> The MDM2 oncoprotein is a cellular inhibitor of the p53 tumor suppressor in that it can bind the transactivation domain of p53 and downregulate its ability to activate transcription. In certain cancers, MDM2 amplification is a common event and contributes to the inactivation of p53. The crystal structure of the 109-residue amino-terminal domain of MDM2 bound to 109-residue transactivation domain peptide of p53 revealed that MDM2 has a &lt;scene name='Matt_Routh_sandbox/Hydrophobic_cavity/1'&gt;deep hydrophobic cleft&lt;/scene&gt; on which the p53 peptide binds as an amphipathic alpha helix. The interface relies on the steric complementarity between the MDM2 cleft and the hydrophobic face of the p53 alpha helix and, in particular, on a triad of p53 amino acids-Phe19, Trp23, and Leu26-which insert &lt;scene name='Matt_Routh_sandbox/Connection_to_p53/5'&gt;deep inside&lt;/scene&gt; the MDM2 cleft. These same p53 residues are also involved in transactivation, supporting the hypothesis that MDM2 inactivates p53 by concealing its transactivation domain. The structure also suggests that the amphipathic alpha helix may be a common structural motif in the binding of a diverse family of transactivation factors to the TATA-binding protein-associated factors.<br /> <br /> Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain., Kussie PH, Gorina S, Marechal V, Elenbaas B, Moreau J, Levine AJ, Pavletich NP, Science. 1996 Nov 8;274(5289):948-53. PMID:8875929<br /> <br /> From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. <br /> <br /> ==Role in Cancer==<br /> MDM2 is an active inhibitor of the p53 anti-tumorgenesis protein. When MDM2 is atached p53 is unable to release transcription factors that code for apoptosis or halting of the cell cycle. The full cell signaling pathway is very complex, but MDM2 is usually activated by <br /> <br /> [[Image:800px-Signal transduction v1.png]]<br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:8875929&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> [[Category: Xenopus laevis]]<br /> [[Category: P53 Tumor Suppressor]]<br /> [[Category: Kussie, P H.]]<br /> [[Category: Pavletich, N P.]]<br /> [[Category: Activator]]<br /> [[Category: Anti-oncogene]]<br /> [[Category: Dna-binding]]<br /> [[Category: Nuclear protein]]<br /> [[Category: Phosphorylation]]<br /> [[Category: Transcription regulation]]</div>

Matt Routh https://proteopedia.org/index.php?title=MDM2&diff=1003156 2009-10-02T00:14:46Z

<p>Matt Routh: </p> <hr /> <div>{{STRUCTURE_1ycq| PDB=1ycq | SCENE= }}<br /> ===MDM2 BOUND TO HUMAN P53 Protein===<br /> ==About MDM2 Structure==<br /> The MDM2 oncoprotein is a cellular inhibitor of the p53 tumor suppressor in that it can bind the transactivation domain of p53 and downregulate its ability to activate transcription. In certain cancers, MDM2 amplification is a common event and contributes to the inactivation of p53. The crystal structure of the 109-residue amino-terminal domain of MDM2 bound to 109-residue transactivation domain peptide of p53 revealed that MDM2 has a deep hydrophobic cleft on which the p53 peptide binds as an amphipathic alpha helix. The interface relies on the steric complementarity between the MDM2 cleft and the hydrophobic face of the p53 alpha helix and, in particular, on a triad of p53 amino acids-Phe19, Trp23, and Leu26-which insert &lt;scene name='Matt_Routh_sandbox/Connection_to_p53/5'&gt;deep inside&lt;/scene&gt; the MDM2 cleft. These same p53 residues are also involved in transactivation, supporting the hypothesis that MDM2 inactivates p53 by concealing its transactivation domain. The structure also suggests that the amphipathic alpha helix may be a common structural motif in the binding of a diverse family of transactivation factors to the TATA-binding protein-associated factors.<br /> <br /> Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain., Kussie PH, Gorina S, Marechal V, Elenbaas B, Moreau J, Levine AJ, Pavletich NP, Science. 1996 Nov 8;274(5289):948-53. PMID:8875929<br /> <br /> From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. <br /> <br /> ==Role in Cancer==<br /> MDM2 is an active inhibitor of the p53 anti-tumorgenesis protein. When MDM2 is atached p53 is unable to release transcription factors that code for apoptosis or halting of the cell cycle. The full cell signaling pathway is very complex, but MDM2 is usually activated by <br /> <br /> [[Image:800px-Signal transduction v1.png]]<br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:8875929&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> [[Category: Xenopus laevis]]<br /> [[Category: P53 Tumor Suppressor]]<br /> [[Category: Kussie, P H.]]<br /> [[Category: Pavletich, N P.]]<br /> [[Category: Activator]]<br /> [[Category: Anti-oncogene]]<br /> [[Category: Dna-binding]]<br /> [[Category: Nuclear protein]]<br /> [[Category: Phosphorylation]]<br /> [[Category: Transcription regulation]]</div>

Matt Routh https://proteopedia.org/index.php?title=MDM2&diff=1003154 2009-10-02T00:11:08Z

<p>Matt Routh: </p> <hr /> <div>{{STRUCTURE_1ycq| PDB=1ycq | SCENE= }}<br /> ===MDM2 BOUND TO HUMAN P53 Protein===<br /> ==About MDM2 Structure==<br /> The MDM2 oncoprotein is a cellular inhibitor of the p53 tumor suppressor in that it can bind the transactivation domain of p53 and downregulate its ability to activate transcription. In certain cancers, MDM2 amplification is a common event and contributes to the inactivation of p53. The crystal structure of the 109-residue amino-terminal domain of MDM2 bound to 109-residue transactivation domain peptide of p53 revealed that MDM2 has a deep hydrophobic cleft on which the p53 peptide binds as an amphipathic alpha helix. The interface relies on the steric complementarity between the MDM2 cleft and the hydrophobic face of the p53 alpha helix and, in particular, on a triad of p53 amino acids-Phe19, Trp23, and Leu26-which insert &lt;scene name='Matt_Routh_sandbox/Connection_to_p53/5'&gt;deep inside&lt;/scene&gt; the MDM2 cleft. These same p53 residues are also involved in transactivation, supporting the hypothesis that MDM2 inactivates p53 by concealing its transactivation domain. The structure also suggests that the amphipathic alpha helix may be a common structural motif in the binding of a diverse family of transactivation factors to the TATA-binding protein-associated factors.<br /> <br /> Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain., Kussie PH, Gorina S, Marechal V, Elenbaas B, Moreau J, Levine AJ, Pavletich NP, Science. 1996 Nov 8;274(5289):948-53. PMID:8875929<br /> <br /> From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. <br /> <br /> {{STRUCTURE_1ycq| SCENE= }}<br /> ==Role in Cancer==<br /> MDM2 is an active inhibitor of the p53 anti-tumorgenesis protein. When MDM2 is atached p53 is unable to release transcription factors that code for apoptosis or halting of the cell cycle. The full cell signaling pathway is very complex, but MDM2 is usually activated by <br /> <br /> [[Image:Image:800px-Signal transduction v1.png]]<br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:8875929&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> [[Category: Xenopus laevis]]<br /> [[Category: P53 Tumor Suppressor]]<br /> [[Category: Kussie, P H.]]<br /> [[Category: Pavletich, N P.]]<br /> [[Category: Activator]]<br /> [[Category: Anti-oncogene]]<br /> [[Category: Dna-binding]]<br /> [[Category: Nuclear protein]]<br /> [[Category: Phosphorylation]]<br /> [[Category: Transcription regulation]]</div>

Matt Routh https://proteopedia.org/index.php?title=File:800px-Signal_transduction_v1.png&diff=1003153 2009-10-02T00:09:26Z

<p>Matt Routh: Detailed overview of signal transduction pathway for apoptosis.</p> <hr /> <div>Detailed overview of signal transduction pathway for apoptosis.</div>

Matt Routh https://proteopedia.org/index.php?title=MDM2&diff=1003152 2009-10-02T00:00:58Z

<p>Matt Routh: </p> <hr /> <div>{{STRUCTURE_1ycq| PDB=1ycq | SCENE= }}<br /> ===MDM2 BOUND TO HUMAN P53 Protein===<br /> ==About MDM2 Structure==<br /> The MDM2 oncoprotein is a cellular inhibitor of the p53 tumor suppressor in that it can bind the transactivation domain of p53 and downregulate its ability to activate transcription. In certain cancers, MDM2 amplification is a common event and contributes to the inactivation of p53. The crystal structure of the 109-residue amino-terminal domain of MDM2 bound to 109-residue transactivation domain peptide of p53 revealed that MDM2 has a deep hydrophobic cleft on which the p53 peptide binds as an amphipathic alpha helix. The interface relies on the steric complementarity between the MDM2 cleft and the hydrophobic face of the p53 alpha helix and, in particular, on a triad of p53 amino acids-Phe19, Trp23, and Leu26-which insert &lt;scene name='Matt_Routh_sandbox/Connection_to_p53/5'&gt;deep inside&lt;/scene&gt; the MDM2 cleft. These same p53 residues are also involved in transactivation, supporting the hypothesis that MDM2 inactivates p53 by concealing its transactivation domain. The structure also suggests that the amphipathic alpha helix may be a common structural motif in the binding of a diverse family of transactivation factors to the TATA-binding protein-associated factors.<br /> <br /> Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain., Kussie PH, Gorina S, Marechal V, Elenbaas B, Moreau J, Levine AJ, Pavletich NP, Science. 1996 Nov 8;274(5289):948-53. PMID:8875929<br /> <br /> From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. <br /> <br /> {{STRUCTURE_1ycq| SCENE= }}<br /> ==Role in Cancer==<br /> MDM2 is an active inhibitor of the p53 anti-tumorgenesis protein. When MDM2 is atached p53 is unable to release transcription factors that code for apoptosis or halting of the cell cycle. The full cell signaling pathway is very complex, but MDM2 is usually activated by <br /> <br /> [[Image:http://genesdev.cshlp.org/content/13/8/916.full]]<br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:8875929&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> [[Category: Xenopus laevis]]<br /> [[Category: P53 Tumor Suppressor]]<br /> [[Category: Kussie, P H.]]<br /> [[Category: Pavletich, N P.]]<br /> [[Category: Activator]]<br /> [[Category: Anti-oncogene]]<br /> [[Category: Dna-binding]]<br /> [[Category: Nuclear protein]]<br /> [[Category: Phosphorylation]]<br /> [[Category: Transcription regulation]]</div>

Matt Routh https://proteopedia.org/index.php?title=MDM2&diff=1003151 2009-10-01T23:57:23Z

<p>Matt Routh: </p> <hr /> <div>{{STRUCTURE_1ycq| PDB=1ycq | SCENE= }}<br /> ===MDM2 BOUND TO HUMAN P53 Protein===<br /> ==About MDM2 Structure==<br /> The MDM2 oncoprotein is a cellular inhibitor of the p53 tumor suppressor in that it can bind the transactivation domain of p53 and downregulate its ability to activate transcription. In certain cancers, MDM2 amplification is a common event and contributes to the inactivation of p53. The crystal structure of the 109-residue amino-terminal domain of MDM2 bound to 109-residue transactivation domain peptide of p53 revealed that MDM2 has a deep hydrophobic cleft on which the p53 peptide binds as an amphipathic alpha helix. The interface relies on the steric complementarity between the MDM2 cleft and the hydrophobic face of the p53 alpha helix and, in particular, on a triad of p53 amino acids-Phe19, Trp23, and Leu26-which insert &lt;scene name='Matt_Routh_sandbox/Connection_to_p53/5'&gt;deep inside&lt;/scene&gt; the MDM2 cleft. These same p53 residues are also involved in transactivation, supporting the hypothesis that MDM2 inactivates p53 by concealing its transactivation domain. The structure also suggests that the amphipathic alpha helix may be a common structural motif in the binding of a diverse family of transactivation factors to the TATA-binding protein-associated factors.<br /> <br /> Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain., Kussie PH, Gorina S, Marechal V, Elenbaas B, Moreau J, Levine AJ, Pavletich NP, Science. 1996 Nov 8;274(5289):948-53. PMID:8875929<br /> <br /> From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. <br /> <br /> ==Role in Cancer==<br /> MDM2 is an active inhibitor of the p53 anti-tumorgenesis protein. When MDM2 is atached p53 is unable to release transcription factors that code for apoptosis or halting of the cell cycle. The full cell signaling pathway is very complex, but MDM2 is usually activated by <br /> <br /> [[Image:http://genesdev.cshlp.org/content/13/8/916.full]]<br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:8875929&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> [[Category: Xenopus laevis]]<br /> [[Category: P53 Tumor Suppressor]]<br /> [[Category: Kussie, P H.]]<br /> [[Category: Pavletich, N P.]]<br /> [[Category: Activator]]<br /> [[Category: Anti-oncogene]]<br /> [[Category: Dna-binding]]<br /> [[Category: Nuclear protein]]<br /> [[Category: Phosphorylation]]<br /> [[Category: Transcription regulation]]</div>

Matt Routh https://proteopedia.org/index.php?title=MDM2&diff=1003150 2009-10-01T23:56:10Z

<p>Matt Routh: </p> <hr /> <div>{{STRUCTURE_1ycq| PDB=1ycq | SCENE= }}<br /> ===MDM2 BOUND TO HUMAN P53 Protein===<br /> ==About MDM2 Structure==<br /> The MDM2 oncoprotein is a cellular inhibitor of the p53 tumor suppressor in that it can bind the transactivation domain of p53 and downregulate its ability to activate transcription. In certain cancers, MDM2 amplification is a common event and contributes to the inactivation of p53. The crystal structure of the 109-residue amino-terminal domain of MDM2 bound to 109-residue transactivation domain peptide of p53 revealed that MDM2 has a deep hydrophobic cleft on which the p53 peptide binds as an amphipathic alpha helix. The interface relies on the steric complementarity between the MDM2 cleft and the hydrophobic face of the p53 alpha helix and, in particular, on a triad of p53 amino acids-Phe19, Trp23, and Leu26-which insert &lt;scene name='Matt_Routh_sandbox/Connection_to_p53/5'&gt;deep inside&lt;/scene&gt; the MDM2 cleft. These same p53 residues are also involved in transactivation, supporting the hypothesis that MDM2 inactivates p53 by concealing its transactivation domain. The structure also suggests that the amphipathic alpha helix may be a common structural motif in the binding of a diverse family of transactivation factors to the TATA-binding protein-associated factors.<br /> <br /> Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain., Kussie PH, Gorina S, Marechal V, Elenbaas B, Moreau J, Levine AJ, Pavletich NP, Science. 1996 Nov 8;274(5289):948-53. PMID:8875929<br /> <br /> From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. <br /> ==Role in Cancer==<br /> MDM2 is an active inhibitor of the p53 anti-tumorgenesis protein. When MDM2 is atached p53 is unable to release transcription factors that code for apoptosis or halting of the cell cycle. The full cell signaling pathway is very complex, but MDM2 is usually activated by <br /> <br /> [[Image:http://genesdev.cshlp.org/content/13/8/916.full]]<br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:8875929&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> [[Category: Xenopus laevis]]<br /> [[Category: P53 Tumor Suppressor]]<br /> [[Category: Kussie, P H.]]<br /> [[Category: Pavletich, N P.]]<br /> [[Category: Activator]]<br /> [[Category: Anti-oncogene]]<br /> [[Category: Dna-binding]]<br /> [[Category: Nuclear protein]]<br /> [[Category: Phosphorylation]]<br /> [[Category: Transcription regulation]]</div>

Matt Routh https://proteopedia.org/index.php?title=MDM2&diff=1003149 2009-10-01T23:31:23Z

<p>Matt Routh: </p> <hr /> <div>{{STRUCTURE_1ycq| PDB=1ycq | SCENE= }}<br /> ===MDM2 BOUND TO HUMAN P53 Protein===<br /> ==About this Structure==<br /> The MDM2 oncoprotein is a cellular inhibitor of the p53 tumor suppressor in that it can bind the transactivation domain of p53 and downregulate its ability to activate transcription. In certain cancers, MDM2 amplification is a common event and contributes to the inactivation of p53. The crystal structure of the 109-residue amino-terminal domain of MDM2 bound to 109-residue transactivation domain peptide of p53 revealed that MDM2 has a deep hydrophobic cleft on which the p53 peptide binds as an amphipathic alpha helix. The interface relies on the steric complementarity between the MDM2 cleft and the hydrophobic face of the p53 alpha helix and, in particular, on a triad of p53 amino acids-Phe19, Trp23, and Leu26-which insert &lt;scene name='Matt_Routh_sandbox/Connection_to_p53/5'&gt;deep inside&lt;/scene&gt; the MDM2 cleft. These same p53 residues are also involved in transactivation, supporting the hypothesis that MDM2 inactivates p53 by concealing its transactivation domain. The structure also suggests that the amphipathic alpha helix may be a common structural motif in the binding of a diverse family of transactivation factors to the TATA-binding protein-associated factors.<br /> <br /> Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain., Kussie PH, Gorina S, Marechal V, Elenbaas B, Moreau J, Levine AJ, Pavletich NP, Science. 1996 Nov 8;274(5289):948-53. PMID:8875929<br /> <br /> From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. <br /> ==Role in Cancer==<br /> [[Image:http://genesdev.cshlp.org/content/13/8/916.full]]<br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:8875929&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> [[Category: Xenopus laevis]]<br /> [[Category: P53 Tumor Suppressor]]<br /> [[Category: Kussie, P H.]]<br /> [[Category: Pavletich, N P.]]<br /> [[Category: Activator]]<br /> [[Category: Anti-oncogene]]<br /> [[Category: Dna-binding]]<br /> [[Category: Nuclear protein]]<br /> [[Category: Phosphorylation]]<br /> [[Category: Transcription regulation]]</div>

Matt Routh https://proteopedia.org/index.php?title=MDM2&diff=1003148 2009-10-01T23:30:36Z

<p>Matt Routh: </p> <hr /> <div>{{STRUCTURE_1ycq| PDB=1ycq | SCENE= }}<br /> ===MDM2 BOUND TO HUMAN P53 Protein===<br /> ==About this Structure==<br /> The MDM2 oncoprotein is a cellular inhibitor of the p53 tumor suppressor in that it can bind the transactivation domain of p53 and downregulate its ability to activate transcription. In certain cancers, MDM2 amplification is a common event and contributes to the inactivation of p53. The crystal structure of the 109-residue amino-terminal domain of MDM2 bound to 109-residue transactivation domain peptide of p53 revealed that MDM2 has a deep hydrophobic cleft on which the p53 peptide binds as an amphipathic alpha helix. The interface relies on the steric complementarity between the MDM2 cleft and the hydrophobic face of the p53 alpha helix and, in particular, on a triad of p53 amino acids-Phe19, Trp23, and Leu26-which insert &lt;scene name='Matt_Routh_sandbox/Connection_to_p53/5'&gt;deep inside&lt;/scene&gt; the MDM2 cleft. These same p53 residues are also involved in transactivation, supporting the hypothesis that MDM2 inactivates p53 by concealing its transactivation domain. The structure also suggests that the amphipathic alpha helix may be a common structural motif in the binding of a diverse family of transactivation factors to the TATA-binding protein-associated factors.<br /> <br /> Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain., Kussie PH, Gorina S, Marechal V, Elenbaas B, Moreau J, Levine AJ, Pavletich NP, Science. 1996 Nov 8;274(5289):948-53. PMID:8875929<br /> <br /> From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. <br /> ==Role in Cancer==<br /> [[Image:F1.medium[1].gif]]<br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:8875929&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> [[Category: Xenopus laevis]]<br /> [[Category: P53 Tumor Suppressor]]<br /> [[Category: Kussie, P H.]]<br /> [[Category: Pavletich, N P.]]<br /> [[Category: Activator]]<br /> [[Category: Anti-oncogene]]<br /> [[Category: Dna-binding]]<br /> [[Category: Nuclear protein]]<br /> [[Category: Phosphorylation]]<br /> [[Category: Transcription regulation]]</div>

Matt Routh https://proteopedia.org/index.php?title=MDM2&diff=996711 2009-09-19T23:39:38Z

<p>Matt Routh: </p> <hr /> <div>{{STRUCTURE_1ycq| PDB=1ycq | SCENE= }}<br /> ===MDM2 BOUND TO HUMAN P53 Protein===<br /> ==About this Structure==<br /> &quot;The MDM2 oncoprotein is a cellular inhibitor of the p53 tumor suppressor in that it can bind the transactivation domain of p53 and downregulate its ability to activate transcription. In certain cancers, MDM2 amplification is a common event and contributes to the inactivation of p53. The crystal structure of the 109-residue amino-terminal domain of MDM2 bound to 109-residue transactivation domain peptide of p53 revealed that MDM2 has a deep hydrophobic cleft on which the p53 peptide binds as an amphipathic alpha helix. The interface relies on the steric complementarity between the MDM2 cleft and the hydrophobic face of the p53 alpha helix and, in particular, on a triad of p53 amino acids-Phe19, Trp23, and Leu26-which insert &lt;scene name='Matt_Routh_sandbox/Connection_to_p53/5'&gt;deep inside&lt;/scene&gt; the MDM2 cleft. These same p53 residues are also involved in transactivation, supporting the hypothesis that MDM2 inactivates p53 by concealing its transactivation domain. The structure also suggests that the amphipathic alpha helix may be a common structural motif in the binding of a diverse family of transactivation factors to the TATA-binding protein-associated factors.&quot;<br /> <br /> Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain., Kussie PH, Gorina S, Marechal V, Elenbaas B, Moreau J, Levine AJ, Pavletich NP, Science. 1996 Nov 8;274(5289):948-53. PMID:8875929<br /> <br /> From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. <br /> <br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:8875929&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> [[Category: Xenopus laevis]]<br /> [[Category: P53 Tumor Suppressor]]<br /> [[Category: Kussie, P H.]]<br /> [[Category: Pavletich, N P.]]<br /> [[Category: Activator]]<br /> [[Category: Anti-oncogene]]<br /> [[Category: Dna-binding]]<br /> [[Category: Nuclear protein]]<br /> [[Category: Phosphorylation]]<br /> [[Category: Transcription regulation]]</div>

Matt Routh https://proteopedia.org/index.php?title=MDM2&diff=996710 2009-09-19T23:34:49Z

<p>Matt Routh: </p> <hr /> <div>{{STRUCTURE_1ycq| PDB=1ycq | SCENE= }}<br /> ===MDM2 BOUND TO HUMAN P53 Protein===<br /> ==About this Structure==<br /> &quot;The MDM2 oncoprotein is a cellular inhibitor of the p53 tumor suppressor in that it can bind the transactivation domain of p53 and downregulate its ability to activate transcription. In certain cancers, MDM2 amplification is a common event and contributes to the inactivation of p53. The crystal structure of the 109-residue amino-terminal domain of MDM2 bound to 109-residue transactivation domain peptide of p53 revealed that MDM2 has a deep hydrophobic cleft on which the p53 peptide binds as an amphipathic alpha helix. The interface relies on the steric complementarity between the MDM2 cleft and the hydrophobic face of the p53 alpha helix and, in particular, on a triad of p53 amino acids-Phe19, Trp23, and Leu26-which insert &lt;scene name='Matt_Routh_sandbox/Connection_to_p53/4'&gt;deep into&lt;/scene&gt; the MDM2 cleft. These same p53 residues are also involved in transactivation, supporting the hypothesis that MDM2 inactivates p53 by concealing its transactivation domain. The structure also suggests that the amphipathic alpha helix may be a common structural motif in the binding of a diverse family of transactivation factors to the TATA-binding protein-associated factors.&quot;<br /> <br /> Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain., Kussie PH, Gorina S, Marechal V, Elenbaas B, Moreau J, Levine AJ, Pavletich NP, Science. 1996 Nov 8;274(5289):948-53. PMID:8875929<br /> <br /> From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. <br /> <br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:8875929&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> [[Category: Xenopus laevis]]<br /> [[Category: P53 Tumor Suppressor]]<br /> [[Category: Kussie, P H.]]<br /> [[Category: Pavletich, N P.]]<br /> [[Category: Activator]]<br /> [[Category: Anti-oncogene]]<br /> [[Category: Dna-binding]]<br /> [[Category: Nuclear protein]]<br /> [[Category: Phosphorylation]]<br /> [[Category: Transcription regulation]]</div>

Matt Routh https://proteopedia.org/index.php?title=MDM2&diff=996709 2009-09-19T23:29:40Z

<p>Matt Routh: </p> <hr /> <div>{{STRUCTURE_1ycq| PDB=1ycq | SCENE= }}<br /> ===MDM2 BOUND TO HUMAN P53 Protein===<br /> ==About this Structure==<br /> &quot;The MDM2 oncoprotein is a cellular inhibitor of the p53 tumor suppressor in that it can bind the transactivation domain of p53 and downregulate its ability to activate transcription. In certain cancers, MDM2 amplification is a common event and contributes to the inactivation of p53. The crystal structure of the 109-residue amino-terminal domain of MDM2 bound to 109-residue transactivation domain peptide of p53 revealed that MDM2 has a deep hydrophobic cleft on which the p53 peptide binds as an amphipathic alpha helix. The interface relies on the steric complementarity between the MDM2 cleft and the hydrophobic face of the p53 alpha helix and, in particular, on a triad of p53 amino acids-Phe19, Trp23, and Leu26-which insert &lt;scene name='Matt_Routh_sandbox/Connection_to_p53/3'&gt;deep into&lt;/scene&gt; the MDM2 cleft. These same p53 residues are also involved in transactivation, supporting the hypothesis that MDM2 inactivates p53 by concealing its transactivation domain. The structure also suggests that the amphipathic alpha helix may be a common structural motif in the binding of a diverse family of transactivation factors to the TATA-binding protein-associated factors.&quot;<br /> <br /> Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain., Kussie PH, Gorina S, Marechal V, Elenbaas B, Moreau J, Levine AJ, Pavletich NP, Science. 1996 Nov 8;274(5289):948-53. PMID:8875929<br /> <br /> From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. <br /> <br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:8875929&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> [[Category: Xenopus laevis]]<br /> [[Category: P53 Tumor Suppressor]]<br /> [[Category: Kussie, P H.]]<br /> [[Category: Pavletich, N P.]]<br /> [[Category: Activator]]<br /> [[Category: Anti-oncogene]]<br /> [[Category: Dna-binding]]<br /> [[Category: Nuclear protein]]<br /> [[Category: Phosphorylation]]<br /> [[Category: Transcription regulation]]</div>

Matt Routh https://proteopedia.org/index.php?title=MDM2&diff=996708 2009-09-19T23:21:07Z

<p>Matt Routh: </p> <hr /> <div>{{STRUCTURE_1ycq| PDB=1ycq | SCENE= }}<br /> ===MDM2 BOUND TO HUMAN P53 Protein===<br /> ==About this Structure==<br /> &quot;The MDM2 oncoprotein is a cellular inhibitor of the p53 tumor suppressor in that it can bind the transactivation domain of p53 and downregulate its ability to activate transcription. In certain cancers, MDM2 amplification is a common event and contributes to the inactivation of p53. The crystal structure of the 109-residue amino-terminal domain of MDM2 bound to 109-residue transactivation domain peptide of p53 revealed that MDM2 has a deep hydrophobic cleft on which the p53 peptide binds as an amphipathic alpha helix. The interface relies on the steric complementarity between the MDM2 cleft and the &lt;scene name='Matt_Routh_sandbox/Hydrophobic_face/1'&gt;hydrophobic face&lt;/scene&gt; of the p53 alpha helix and, in particular, on a triad of p53 amino acids-Phe19, Trp23, and Leu26-which insert deep into the MDM2 cleft. These same p53 residues are also involved in transactivation, supporting the hypothesis that MDM2 inactivates p53 by concealing its transactivation domain. The structure also suggests that the amphipathic alpha helix may be a common structural motif in the binding of a diverse family of transactivation factors to the TATA-binding protein-associated factors.&quot;<br /> <br /> Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain., Kussie PH, Gorina S, Marechal V, Elenbaas B, Moreau J, Levine AJ, Pavletich NP, Science. 1996 Nov 8;274(5289):948-53. PMID:8875929<br /> <br /> From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. <br /> <br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:8875929&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> [[Category: Xenopus laevis]]<br /> [[Category: P53 Tumor Suppressor]]<br /> [[Category: Kussie, P H.]]<br /> [[Category: Pavletich, N P.]]<br /> [[Category: Activator]]<br /> [[Category: Anti-oncogene]]<br /> [[Category: Dna-binding]]<br /> [[Category: Nuclear protein]]<br /> [[Category: Phosphorylation]]<br /> [[Category: Transcription regulation]]</div>

Matt Routh https://proteopedia.org/index.php?title=MDM2&diff=996707 2009-09-19T23:15:46Z

<p>Matt Routh: </p> <hr /> <div>{{STRUCTURE_1ycq| PDB=1ycq | SCENE= }}<br /> ===MDM2 BOUND TO HUMAN P53 Protein===<br /> ==About this Structure==<br /> &quot;The MDM2 oncoprotein is a cellular inhibitor of the p53 tumor suppressor in that it can bind the transactivation domain of p53 and downregulate its ability to activate transcription. In certain cancers, MDM2 amplification is a common event and contributes to the inactivation of p53. The crystal structure of the &lt;scene name='Matt_Routh_sandbox/Connection_to_p53/1'&gt;109-residue&lt;/scene&gt; amino-terminal domain of MDM2 bound to a 15-residue transactivation domain peptide of p53 revealed that MDM2 has a deep hydrophobic cleft on which the p53 peptide binds as an amphipathic alpha helix. The interface relies on the steric complementarity between the MDM2 cleft and the &lt;scene name='Matt_Routh_sandbox/Hydrophobic_face/1'&gt;hydrophobic face&lt;/scene&gt; of the p53 alpha helix and, in particular, on a triad of p53 amino acids-Phe19, Trp23, and Leu26-which insert deep into the MDM2 cleft. These same p53 residues are also involved in transactivation, supporting the hypothesis that MDM2 inactivates p53 by concealing its transactivation domain. The structure also suggests that the amphipathic alpha helix may be a common structural motif in the binding of a diverse family of transactivation factors to the TATA-binding protein-associated factors.&quot;<br /> <br /> Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain., Kussie PH, Gorina S, Marechal V, Elenbaas B, Moreau J, Levine AJ, Pavletich NP, Science. 1996 Nov 8;274(5289):948-53. PMID:8875929<br /> <br /> From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. <br /> <br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:8875929&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> [[Category: Xenopus laevis]]<br /> [[Category: P53 Tumor Suppressor]]<br /> [[Category: Kussie, P H.]]<br /> [[Category: Pavletich, N P.]]<br /> [[Category: Activator]]<br /> [[Category: Anti-oncogene]]<br /> [[Category: Dna-binding]]<br /> [[Category: Nuclear protein]]<br /> [[Category: Phosphorylation]]<br /> [[Category: Transcription regulation]]</div>

Matt Routh https://proteopedia.org/index.php?title=MDM2&diff=996706 2009-09-19T21:22:24Z

<p>Matt Routh: </p> <hr /> <div>{{STRUCTURE_1ycq| PDB=1ycq | SCENE= }}<br /> ===MDM2 BOUND TO HUMAN P53 Protein===<br /> ==About this Structure==<br /> &quot;The MDM2 oncoprotein is a cellular inhibitor of the p53 tumor suppressor in that it can bind the transactivation domain of p53 and downregulate its ability to activate transcription. In certain cancers, MDM2 amplification is a common event and contributes to the inactivation of p53. The crystal structure of the &lt;scene name='Matt_Routh_sandbox/Connection_to_p53/1'&gt;109-residue&lt;/scene&gt; amino-terminal domain of MDM2 bound to a 15-residue transactivation domain peptide of p53 revealed that MDM2 has a deep hydrophobic cleft on which the p53 peptide binds as an amphipathic alpha helix. The interface relies on the steric complementarity between the MDM2 cleft and the hydrophobic face of the p53 alpha helix and, in particular, on a triad of p53 amino acids-Phe19, Trp23, and Leu26-which insert deep into the MDM2 cleft. These same p53 residues are also involved in transactivation, supporting the hypothesis that MDM2 inactivates p53 by concealing its transactivation domain. The structure also suggests that the amphipathic alpha helix may be a common structural motif in the binding of a diverse family of transactivation factors to the TATA-binding protein-associated factors.&quot;<br /> <br /> Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain., Kussie PH, Gorina S, Marechal V, Elenbaas B, Moreau J, Levine AJ, Pavletich NP, Science. 1996 Nov 8;274(5289):948-53. PMID:8875929<br /> <br /> From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. <br /> <br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:8875929&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> [[Category: Xenopus laevis]]<br /> [[Category: P53 Tumor Suppressor]]<br /> [[Category: Kussie, P H.]]<br /> [[Category: Pavletich, N P.]]<br /> [[Category: Activator]]<br /> [[Category: Anti-oncogene]]<br /> [[Category: Dna-binding]]<br /> [[Category: Nuclear protein]]<br /> [[Category: Phosphorylation]]<br /> [[Category: Transcription regulation]]</div>

Matt Routh https://proteopedia.org/index.php?title=MDM2&diff=996705 2009-09-19T21:21:10Z

<p>Matt Routh: </p> <hr /> <div>===MDM2 BOUND TO HUMAN P53 Protein===<br /> ==About this Structure==<br /> &quot;The MDM2 oncoprotein is a cellular inhibitor of the p53 tumor suppressor in that it can bind the transactivation domain of p53 and downregulate its ability to activate transcription. In certain cancers, MDM2 amplification is a common event and contributes to the inactivation of p53. The crystal structure of the &lt;scene name='Matt_Routh_sandbox/Connection_to_p53/1'&gt;109-residue&lt;/scene&gt; amino-terminal domain of MDM2 bound to a 15-residue transactivation domain peptide of p53 revealed that MDM2 has a deep hydrophobic cleft on which the p53 peptide binds as an amphipathic alpha helix. The interface relies on the steric complementarity between the MDM2 cleft and the hydrophobic face of the p53 alpha helix and, in particular, on a triad of p53 amino acids-Phe19, Trp23, and Leu26-which insert deep into the MDM2 cleft. These same p53 residues are also involved in transactivation, supporting the hypothesis that MDM2 inactivates p53 by concealing its transactivation domain. The structure also suggests that the amphipathic alpha helix may be a common structural motif in the binding of a diverse family of transactivation factors to the TATA-binding protein-associated factors.&quot;<br /> <br /> Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain., Kussie PH, Gorina S, Marechal V, Elenbaas B, Moreau J, Levine AJ, Pavletich NP, Science. 1996 Nov 8;274(5289):948-53. PMID:8875929<br /> <br /> From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. <br /> <br /> {{STRUCTURE_1ycq| PDB=1ycq | SCENE= }}<br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:8875929&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> [[Category: Xenopus laevis]]<br /> [[Category: P53 Tumor Suppressor]]<br /> [[Category: Kussie, P H.]]<br /> [[Category: Pavletich, N P.]]<br /> [[Category: Activator]]<br /> [[Category: Anti-oncogene]]<br /> [[Category: Dna-binding]]<br /> [[Category: Nuclear protein]]<br /> [[Category: Phosphorylation]]<br /> [[Category: Transcription regulation]]</div>

Matt Routh https://proteopedia.org/index.php?title=MDM2&diff=996704 2009-09-19T21:20:26Z

<p>Matt Routh: </p> <hr /> <div>===MDM2 BOUND TO HUMAN P53 Protein===<br /> ==About this Structure==<br /> &quot;The MDM2 oncoprotein is a cellular inhibitor of the p53 tumor suppressor in that it can bind the transactivation domain of p53 and downregulate its ability to activate transcription. In certain cancers, MDM2 amplification is a common event and contributes to the inactivation of p53. The crystal structure of the &lt;scene name='Matt_Routh_sandbox/Connection_to_p53/1'&gt;109-residue&lt;/scene&gt;<br /> amino-terminal domain of MDM2 bound to a 15-residue transactivation domain peptide of p53 revealed that MDM2 has a deep hydrophobic cleft on which the p53 peptide binds as an amphipathic alpha helix. The interface relies on the steric complementarity between the MDM2 cleft and the hydrophobic face of the p53 alpha helix and, in particular, on a triad of p53 amino acids-Phe19, Trp23, and Leu26-which insert deep into the MDM2 cleft. These same p53 residues are also involved in transactivation, supporting the hypothesis that MDM2 inactivates p53 by concealing its transactivation domain. The structure also suggests that the amphipathic alpha helix may be a common structural motif in the binding of a diverse family of transactivation factors to the TATA-binding protein-associated factors.&quot;<br /> <br /> Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain., Kussie PH, Gorina S, Marechal V, Elenbaas B, Moreau J, Levine AJ, Pavletich NP, Science. 1996 Nov 8;274(5289):948-53. PMID:8875929<br /> <br /> From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. <br /> <br /> {{STRUCTURE_1ycq| PDB=1ycq | SCENE= }}<br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:8875929&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> [[Category: Xenopus laevis]]<br /> [[Category: P53 Tumor Suppressor]]<br /> [[Category: Kussie, P H.]]<br /> [[Category: Pavletich, N P.]]<br /> [[Category: Activator]]<br /> [[Category: Anti-oncogene]]<br /> [[Category: Dna-binding]]<br /> [[Category: Nuclear protein]]<br /> [[Category: Phosphorylation]]<br /> [[Category: Transcription regulation]]</div>

Matt Routh https://proteopedia.org/index.php?title=MDM2&diff=996703 2009-09-19T21:19:16Z

<p>Matt Routh: </p> <hr /> <div>===MDM2 BOUND TO HUMAN P53 Protein===<br /> ==About this Structure==<br /> The MDM2 oncoprotein is a cellular inhibitor of the p53 tumor suppressor in that it can bind the transactivation domain of p53 and downregulate its ability to activate transcription. In certain cancers, MDM2 amplification is a common event and contributes to the inactivation of p53. The crystal structure of the &lt;scene name='Matt_Routh_sandbox/Connection_to_p53/1'&gt;109-residue&lt;/scene&gt;<br /> amino-terminal domain of MDM2 bound to a 15-residue transactivation domain peptide of p53 revealed that MDM2 has a deep hydrophobic cleft on which the p53 peptide binds as an amphipathic alpha helix. The interface relies on the steric complementarity between the MDM2 cleft and the hydrophobic face of the p53 alpha helix and, in particular, on a triad of p53 amino acids-Phe19, Trp23, and Leu26-which insert deep into the MDM2 cleft. These same p53 residues are also involved in transactivation, supporting the hypothesis that MDM2 inactivates p53 by concealing its transactivation domain. The structure also suggests that the amphipathic alpha helix may be a common structural motif in the binding of a diverse family of transactivation factors to the TATA-binding protein-associated factors.<br /> <br /> Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain., Kussie PH, Gorina S, Marechal V, Elenbaas B, Moreau J, Levine AJ, Pavletich NP, Science. 1996 Nov 8;274(5289):948-53. PMID:8875929<br /> <br /> From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. <br /> <br /> {{STRUCTURE_1ycq| PDB=1ycq | SCENE= }}<br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:8875929&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> [[Category: Xenopus laevis]]<br /> [[Category: P53 Tumor Suppressor]]<br /> [[Category: Kussie, P H.]]<br /> [[Category: Pavletich, N P.]]<br /> [[Category: Activator]]<br /> [[Category: Anti-oncogene]]<br /> [[Category: Dna-binding]]<br /> [[Category: Nuclear protein]]<br /> [[Category: Phosphorylation]]<br /> [[Category: Transcription regulation]]</div>

Matt Routh https://proteopedia.org/index.php?title=MDM2&diff=996702 2009-09-19T21:17:02Z

<p>Matt Routh: </p> <hr /> <div>{{STRUCTURE_1ycq| PDB=1ycq | SCENE= }}<br /> <br /> ===MDM2 BOUND TO HUMAN P53 Protein===<br /> ==About this Structure==<br /> The MDM2 oncoprotein is a cellular inhibitor of the p53 tumor suppressor in that it can bind the transactivation domain of p53 and downregulate its ability to activate transcription. In certain cancers, MDM2 amplification is a common event and contributes to the inactivation of p53. The crystal structure of the &lt;scene name='Matt_Routh_sandbox/Connection_to_p53/1'&gt;109-residue&lt;/scene&gt;<br /> amino-terminal domain of MDM2 bound to a 15-residue transactivation domain peptide of p53 revealed that MDM2 has a deep hydrophobic cleft on which the p53 peptide binds as an amphipathic alpha helix. The interface relies on the steric complementarity between the MDM2 cleft and the hydrophobic face of the p53 alpha helix and, in particular, on a triad of p53 amino acids-Phe19, Trp23, and Leu26-which insert deep into the MDM2 cleft. These same p53 residues are also involved in transactivation, supporting the hypothesis that MDM2 inactivates p53 by concealing its transactivation domain. The structure also suggests that the amphipathic alpha helix may be a common structural motif in the binding of a diverse family of transactivation factors to the TATA-binding protein-associated factors.<br /> <br /> Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain., Kussie PH, Gorina S, Marechal V, Elenbaas B, Moreau J, Levine AJ, Pavletich NP, Science. 1996 Nov 8;274(5289):948-53. PMID:8875929<br /> <br /> From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. <br /> <br /> <br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:8875929&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> [[Category: Xenopus laevis]]<br /> [[Category: P53 Tumor Suppressor]]<br /> [[Category: Kussie, P H.]]<br /> [[Category: Pavletich, N P.]]<br /> [[Category: Activator]]<br /> [[Category: Anti-oncogene]]<br /> [[Category: Dna-binding]]<br /> [[Category: Nuclear protein]]<br /> [[Category: Phosphorylation]]<br /> [[Category: Transcription regulation]]</div>

Matt Routh https://proteopedia.org/index.php?title=MDM2&diff=996701 2009-09-19T21:16:10Z

<p>Matt Routh: </p> <hr /> <div>{{STRUCTURE_1ycq| PDB=1ycq | SCENE= }}<br /> <br /> ===MDM2 BOUND TO HUMAN P53 Protein===<br /> <br /> {{ABSTRACT_PUBMED_8875929}}<br /> <br /> ==About this Structure==<br /> The MDM2 oncoprotein is a cellular inhibitor of the p53 tumor suppressor in that it can bind the transactivation domain of p53 and downregulate its ability to activate transcription. In certain cancers, MDM2 amplification is a common event and contributes to the inactivation of p53. The crystal structure of the &lt;scene name='Matt_Routh_sandbox/Connection_to_p53/1'&gt;109-residue&lt;/scene&gt;<br /> amino-terminal domain of MDM2 bound to a 15-residue transactivation domain peptide of p53 revealed that MDM2 has a deep hydrophobic cleft on which the p53 peptide binds as an amphipathic alpha helix. The interface relies on the steric complementarity between the MDM2 cleft and the hydrophobic face of the p53 alpha helix and, in particular, on a triad of p53 amino acids-Phe19, Trp23, and Leu26-which insert deep into the MDM2 cleft. These same p53 residues are also involved in transactivation, supporting the hypothesis that MDM2 inactivates p53 by concealing its transactivation domain. The structure also suggests that the amphipathic alpha helix may be a common structural motif in the binding of a diverse family of transactivation factors to the TATA-binding protein-associated factors.<br /> <br /> Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain., Kussie PH, Gorina S, Marechal V, Elenbaas B, Moreau J, Levine AJ, Pavletich NP, Science. 1996 Nov 8;274(5289):948-53. PMID:8875929<br /> <br /> From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. <br /> <br /> <br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:8875929&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> [[Category: Xenopus laevis]]<br /> [[Category: P53 Tumor Suppressor]]<br /> [[Category: Kussie, P H.]]<br /> [[Category: Pavletich, N P.]]<br /> [[Category: Activator]]<br /> [[Category: Anti-oncogene]]<br /> [[Category: Dna-binding]]<br /> [[Category: Nuclear protein]]<br /> [[Category: Phosphorylation]]<br /> [[Category: Transcription regulation]]</div>

Matt Routh https://proteopedia.org/index.php?title=MDM2&diff=996700 2009-09-19T21:15:00Z

<p>Matt Routh: </p> <hr /> <div>{{STRUCTURE_1ycq| PDB=1ycq | SCENE= }}<br /> <br /> ===MDM2 BOUND TO HUMAN P53 Protein===<br /> <br /> {{ABSTRACT_PUBMED_8875929}}<br /> <br /> ==About this Structure==<br /> 1YCQ is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. The July 2002 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''p53 Tumor Suppressor'' by David S. Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2002_7 10.2210/rcsb_pdb/mom_2002_7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YCQ OCA]. <br /> <br /> &lt;scene name='Matt_Routh_sandbox/Connection_to_p53/1'&gt;109-residue&lt;/scene&gt;<br /> <br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:8875929&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> [[Category: Xenopus laevis]]<br /> [[Category: P53 Tumor Suppressor]]<br /> [[Category: Kussie, P H.]]<br /> [[Category: Pavletich, N P.]]<br /> [[Category: Activator]]<br /> [[Category: Anti-oncogene]]<br /> [[Category: Dna-binding]]<br /> [[Category: Nuclear protein]]<br /> [[Category: Phosphorylation]]<br /> [[Category: Transcription regulation]]</div>

Matt Routh https://proteopedia.org/index.php?title=MDM2&diff=996699 2009-09-19T21:05:52Z

<p>Matt Routh: </p> <hr /> <div>{{STRUCTURE_1ycq| PDB=1ycq | SCENE= }}<br /> <br /> ===MDM2 BOUND TO HUMAN P53 Protein===<br /> <br /> {{ABSTRACT_PUBMED_8875929}}<br /> <br /> ==About this Structure==<br /> 1YCQ is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. The July 2002 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''p53 Tumor Suppressor'' by David S. Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2002_7 10.2210/rcsb_pdb/mom_2002_7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YCQ OCA]. <br /> <br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:8875929&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> [[Category: Xenopus laevis]]<br /> [[Category: P53 Tumor Suppressor]]<br /> [[Category: Kussie, P H.]]<br /> [[Category: Pavletich, N P.]]<br /> [[Category: Activator]]<br /> [[Category: Anti-oncogene]]<br /> [[Category: Dna-binding]]<br /> [[Category: Nuclear protein]]<br /> [[Category: Phosphorylation]]<br /> [[Category: Transcription regulation]]</div>

Matt Routh https://proteopedia.org/index.php?title=MDM2&diff=996698 2009-09-19T21:05:20Z

<p>Matt Routh: </p> <hr /> <div>==This is a placeholder==<br /> This is a placeholder text to help you get started in <br /> placing a Jmol applet on your page. At any time, click<br /> &quot;Show Preview&quot; at the bottom of this page to see how it goes.<br /> <br /> Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load <br /> and display another structure.<br /> <br /> {{STRUCTURE_1ycq| PDB=1ycq | SCENE= }}<br /> <br /> ===MDM2 BOUND TO HUMAN P53 Protein===<br /> <br /> {{ABSTRACT_PUBMED_8875929}}<br /> <br /> ==About this Structure==<br /> 1YCQ is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. The July 2002 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''p53 Tumor Suppressor'' by David S. Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2002_7 10.2210/rcsb_pdb/mom_2002_7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YCQ OCA]. <br /> <br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:8875929&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> [[Category: Xenopus laevis]]<br /> [[Category: P53 Tumor Suppressor]]<br /> [[Category: Kussie, P H.]]<br /> [[Category: Pavletich, N P.]]<br /> [[Category: Activator]]<br /> [[Category: Anti-oncogene]]<br /> [[Category: Dna-binding]]<br /> [[Category: Nuclear protein]]<br /> [[Category: Phosphorylation]]<br /> [[Category: Transcription regulation]]</div>

Matt Routh https://proteopedia.org/index.php?title=MDM2&diff=996697 2009-09-19T21:04:11Z

<p>Matt Routh: </p> <hr /> <div>==This is a placeholder==<br /> This is a placeholder text to help you get started in <br /> placing a Jmol applet on your page. At any time, click<br /> &quot;Show Preview&quot; at the bottom of this page to see how it goes.<br /> <br /> Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load <br /> and display another structure.<br /> <br /> {{STRUCTURE_1ycq| PDB=1ycq | SCENE= }}<br /> <br /> ===XENOPUS LAEVIS MDM2 BOUND TO THE TRANSACTIVATION DOMAIN OF HUMAN P53===<br /> <br /> {{ABSTRACT_PUBMED_8875929}}<br /> <br /> ==About this Structure==<br /> 1YCQ is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. The July 2002 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''p53 Tumor Suppressor'' by David S. Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2002_7 10.2210/rcsb_pdb/mom_2002_7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YCQ OCA]. <br /> <br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:8875929&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> [[Category: Xenopus laevis]]<br /> [[Category: P53 Tumor Suppressor]]<br /> [[Category: Kussie, P H.]]<br /> [[Category: Pavletich, N P.]]<br /> [[Category: Activator]]<br /> [[Category: Anti-oncogene]]<br /> [[Category: Dna-binding]]<br /> [[Category: Nuclear protein]]<br /> [[Category: Phosphorylation]]<br /> [[Category: Transcription regulation]]</div>

Matt Routh https://proteopedia.org/index.php?title=MDM2&diff=996696 2009-09-19T21:01:10Z

<p>Matt Routh: </p> <hr /> <div>==This is a placeholder==<br /> This is a placeholder text to help you get started in <br /> placing a Jmol applet on your page. At any time, click<br /> &quot;Show Preview&quot; at the bottom of this page to see how it goes.<br /> <br /> Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load <br /> and display another structure.<br /> <br /> {{STRUCTURE_1ttv | PDB=1ttv | SCENE= }}</div>

Matt Routh https://proteopedia.org/index.php?title=MDM2&diff=996695 2009-09-19T21:00:38Z

<p>Matt Routh: </p> <hr /> <div>==This is a placeholder==<br /> This is a placeholder text to help you get started in <br /> placing a Jmol applet on your page. At any time, click<br /> &quot;Show Preview&quot; at the bottom of this page to see how it goes.<br /> <br /> Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load <br /> and display another structure.<br /> <br /> {{STRUCTURE_MDM2 | PDB=1ttv | SCENE= }}</div>

Matt Routh https://proteopedia.org/index.php?title=MDM2&diff=996694 2009-09-19T20:59:31Z

<p>Matt Routh: New page: ==This is a placeholder== This is a placeholder text to help you get started in placing a Jmol applet on your page. At any time, click &quot;Show Preview&quot; at the bottom of this page to see how...</p> <hr /> <div>==This is a placeholder==<br /> This is a placeholder text to help you get started in <br /> placing a Jmol applet on your page. At any time, click<br /> &quot;Show Preview&quot; at the bottom of this page to see how it goes.<br /> <br /> Replace the PDB id (use lowercase!) after the STRUCTURE_ and after PDB= to load <br /> and display another structure.<br /> <br /> {{STRUCTURE_3cin | PDB=1ttv | SCENE= }}</div>

Matt Routh https://proteopedia.org/index.php?title=Ann_Taylor_Sandbox_7&diff=990829 2009-09-01T14:56:36Z

<p>Matt Routh: </p> <hr /> <div><br /> [[Image:3d06.jpg|left|200px]]<br /> <br /> &lt;!--<br /> The line below this paragraph, containing &quot;STRUCTURE_3d06&quot;, creates the &quot;Structure Box&quot; on the page.<br /> You may change the PDB parameter (which sets the PDB file loaded into the applet) <br /> or the SCENE parameter (which sets the initial scene displayed when the page is loaded),<br /> or leave the SCENE parameter empty for the default display.<br /> --&gt;<br /> {{STRUCTURE_3d06| PDB=3d06 | SCENE= }} <br /> <br /> ===Human p53 core domain with hot spot mutation R249S (I)===<br /> <br /> <br /> The tumor suppressor protein p53 is mutated in more than 50% of invasive cancers. About 30% of the mutations are found in six major &quot;hot spot&quot; codons located in its DNA binding core domain. To gain structural insight into the deleterious effects of such mutations and their rescue by suppressor mutations, we determined the crystal structures of the p53 core domain incorporating the hot spot mutation &lt;scene name='Ann_Taylor_Sandbox_7/R249s/1'&gt;R249S&lt;/scene&gt;, the core domain incorporating R249S and a second-site suppressor mutation H168R (referred to as the double mutant R249S/H168R) and its sequence-specific complex with DNA and of the triple mutant R249S/H168R/T123A. The structural studies were accompanied by transactivation and apoptosis experiments. The crystal structures show that the region at the vicinity of the mutation site in the R249S mutant displays a range of conformations [wild-type (wt) and several mutant-type conformations] due to the loss of stabilizing interactions mediated by R249 in the wt protein. As a consequence, the protein surface that is critical to the formation of functional p53-DNA complexes, through protein-protein and protein-DNA interactions, is largely distorted in the mutant conformations, thus explaining the protein's &quot;loss of function&quot; as a transcription factor. The structure of this region is restored in both R249S/H168R and R249S/H168R/T123A and is further stabilized in the complex of R249S/H168R with DNA. Our functional data show that the introduction of H168R as a second-site suppressor mutation partially restores the transactivation capacity of the protein and that this effect is further amplified by the addition of a third-site mutation T123A. These findings together with previously reported data on wt and mutant p53 provide a structural framework for understanding p53 dysfunction as a result of oncogenic mutations and its rescue by suppressor mutations and for a potential drug design aimed at restoring wt activity to aberrant p53 proteins. <br /> <br /> Structural basis of restoring sequence-specific DNA binding and transactivation to mutant p53 by suppressor mutations., Suad O, Rozenberg H, Brosh R, Diskin-Posner Y, Kessler N, Shimon LJ, Frolow F, Liran A, Rotter V, Shakked Z, J Mol Biol. 2009 Jan 9;385(1):249-65. Epub 2008 Oct 30. PMID:18996393 <br /> <br /> From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. <br /> <br /> <br /> <br /> ==Disease==<br /> Known disease associated with this structure: Adrenal cortical carcinoma OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191170 191170]], Breast cancer OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191170 191170]], Colorectal cancer OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191170 191170]], Hepatocellular carcinoma OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191170 191170]], Histiocytoma OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191170 191170]], Li-Fraumeni syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191170 191170]], Multiple malignancy syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191170 191170]], Nasopharyngeal carcinoma OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191170 191170]], Osteosarcoma OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191170 191170]], Pancreatic cancer OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191170 191170]], Thyroid carcinoma OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=191170 191170]]<br /> <br /> ==About this Structure==<br /> 3D06 is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D06 OCA]. <br /> <br /> ==Reference==<br /> &lt;ref group=&quot;xtra&quot;&gt;PMID:18996393&lt;/ref&gt;&lt;references group=&quot;xtra&quot;/&gt;<br /> [[Category: Homo sapiens]]<br /> [[Category: Frolow, F.]]<br /> [[Category: Rozenberg, H.]]<br /> [[Category: Shakked, Z.]]<br /> [[Category: Shimon, L J.W.]]<br /> [[Category: Suad, O.]]<br /> [[Category: Acetylation]]<br /> [[Category: Activator]]<br /> [[Category: Alternative splicing]]<br /> [[Category: Anti-oncogene]]<br /> [[Category: Apoptosis]]<br /> [[Category: Cell cycle]]<br /> [[Category: Covalent protein-rna linkage]]<br /> [[Category: Cytoplasm]]<br /> [[Category: Disease mutation]]<br /> [[Category: Dna-binding]]<br /> [[Category: Endoplasmic reticulum]]<br /> [[Category: Glycoprotein]]<br /> [[Category: Host-virus interaction]]<br /> [[Category: Li-fraumeni syndrome]]<br /> [[Category: Loop-sheet-helix motif]]<br /> [[Category: Metal-binding]]<br /> [[Category: Methylation]]<br /> [[Category: Mutant protein]]<br /> [[Category: Nucleus]]<br /> [[Category: P53]]<br /> [[Category: Phosphoprotein]]<br /> [[Category: Polymorphism]]<br /> [[Category: Transcription]]<br /> [[Category: Transcription regulation]]<br /> [[Category: Ubl conjugation]]<br /> [[Category: Zinc]]<br /> <br /> ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 21 10:44:12 2009''</div>

Matt Routh