1b07: Difference between revisions

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{{Seed}}
[[Image:1b07.png|left|200px]]


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==CRK SH3 DOMAIN COMPLEXED WITH PEPTOID INHIBITOR==
The line below this paragraph, containing "STRUCTURE_1b07", creates the "Structure Box" on the page.
<StructureSection load='1b07' size='340' side='right'caption='[[1b07]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1b07]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B07 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1B07 FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PYJ:PHENYLETHANE'>PYJ</scene></td></tr>
{{STRUCTURE_1b07|  PDB=1b07  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1b07 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b07 OCA], [https://pdbe.org/1b07 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1b07 RCSB], [https://www.ebi.ac.uk/pdbsum/1b07 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1b07 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CRK_MOUSE CRK_MOUSE] The Crk-I and Crk-II forms differ in their biological activities. Crk-II has less transforming activity than Crk-I. Crk-II mediates attachment-induced MAPK8 activation, membrane ruffling and cell motility in a Rac-dependent manner. Involved in phagocytosis of apoptotic cells and cell motility via its interaction with DOCK1 and DOCK4. May regulate the EFNA5-EPHA3 signaling.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/b0/1b07_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1b07 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Src homology 3 (SH3) and WW protein interaction domains bind specific proline-rich sequences. However, instead of recognizing critical prolines on the basis of side chain shape or rigidity, these domains broadly accepted amide N-substituted residues. Proline is apparently specifically selected in vivo, despite low complementarity, because it is the only endogenous N-substituted amino acid. This discriminatory mechanism explains how these domains achieve specific but low-affinity recognition, a property that is necessary for transient signaling interactions. The mechanism can be exploited: screening a series of ligands in which key prolines were replaced by nonnatural N-substituted residues yielded a ligand that selectively bound the Grb2 SH3 domain with 100 times greater affinity.


===CRK SH3 DOMAIN COMPLEXED WITH PEPTOID INHIBITOR===
Exploiting the basis of proline recognition by SH3 and WW domains: design of N-substituted inhibitors.,Nguyen JT, Turck CW, Cohen FE, Zuckermann RN, Lim WA Science. 1998 Dec 11;282(5396):2088-92. PMID:9851931<ref>PMID:9851931</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1b07" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_9851931}}, adds the Publication Abstract to the page
*[[Adapter molecule crk 3D structures|Adapter molecule crk 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 9851931 is the PubMed ID number.
*[[Non-Standard Residue|Non-Standard Residue]]
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== References ==
{{ABSTRACT_PUBMED_9851931}}
<references/>
 
__TOC__
==About this Structure==
</StructureSection>
1B07 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B07 OCA].
[[Category: Large Structures]]
 
==Reference==
Exploiting the basis of proline recognition by SH3 and WW domains: design of N-substituted inhibitors., Nguyen JT, Turck CW, Cohen FE, Zuckermann RN, Lim WA, Science. 1998 Dec 11;282(5396):2088-92. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9851931 9851931]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Cohen FE]]
[[Category: Cohen, F E.]]
[[Category: Lim WA]]
[[Category: Lim, W A.]]
[[Category: Nguyen JT]]
[[Category: Nguyen, J T.]]
[[Category: Turck CW]]
[[Category: Turck, C W.]]
[[Category: Zuckermann RN]]
[[Category: Zuckermann, R N.]]
[[Category: Inhibitor]]
[[Category: Peptoid]]
[[Category: Proline-rich motif]]
[[Category: Protein-protein recognition]]
[[Category: Sh3 domain]]
[[Category: Signal transduction]]
 
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Retrieved from "https://proteopedia.org/1b07"