Proteopedia - User contributions [en]

Molecular Playground/Transferrin

2014-12-01T16:17:20Z

Jake Pawlowski:

<Structure load='2HAU' size='500' frame='true' align='right' caption='Human Se-Met transferrin complex with citrate and glycerol [[2hau]]' scene='Insert optional scene name here' />One of the CBI Molecules being studied in the University of Massachusetts Amherst Chemistry-Biology Interface Program at UMass Amherst and on display at the Molecular Playground.

<scene name='User:Khaja_Muneeruddin/Sandbox_1/Apotf/2'>Human Transferrin (hTf)</scene> is a 80 KDa bilobal, iron binding glycoprotein found in blood. In Apo hTf (iron free form), N-lobe (brown) and C-lobe (green) bind one ferric ion each to regulate the concentration of free iron in blood and also transport to iron requiring cells.

N-lobe and C-lobe are homologous and contain identical iron binding amino acid residues. Structurally both N-lobe and C-lobe contain two sub domains namely NI and NII, and CI and CII which come together to form a cleft for binding iron. At the <scene name='User:Khaja_Muneeruddin/Sandbox_1/Nlobe_binding_sites/3'>binding site of N-lobe</scene> Asp63, Tyr188, Tyr95, His249 and Arg124 are involved in trapping of iron<ref>PMID: 9609685</ref>. The amino acids involved in trapping of iron at the <scene name='47/477021/N_lobe_fe_release/3'>binding site</scene> of C-lobe include Asp392, Tyr426, Tyr517, His585, Arg456<ref>PMID: 15924420</ref>. In addition to these amino acids, at both the lobes a carbonate ion also plays an important role in binding iron. At low pH iron is released from N-lobe by protonation of <scene name='Molecular_Playground/Transferrin/N_lobe_fe_release/2'>Lysines</scene> 206 and 296 <ref>PMID: 9609685</ref> and Lys534 and Arg632 in C-lobe.<ref>PMID: 19917294</ref>

After binding iron N-lobe and C-lobe undergo a conformational change. In ApohTf, N lobe has an <scene name='User:Khaja_Muneeruddin/Sandbox_1/Opennlobe/2'>open conformation</scene> and upon binding ferric ion it shows a <scene name='User:Khaja_Muneeruddin/Sandbox_1/Closed/2'>closed conformation</scene> characterized by rotation of N-II sub domain by 63°<ref>PMID: 9760232</ref>. C-lobe also undergo a similar conformational change upon binding ferric ion, however crystal structure information of the C lobe of hTf is limited due to difficulty in production<ref>PMID: 9337853</ref>.

Intracellular delivery of iron by transferrin is carried out by clathrin-dependent receptor-mediated endocytosis. At pH 7.4 diferric human transferrin binds to human transferrin receptor (hTfR). Upon binding, diferric hTf-hTfR is internalized and in the acidic condition of endosome iron is release from diferric hTf-hTfR complex into the cells. Apo hTf-hTfR complex is recycled back to the cell surface and at pH of cell surface Tf dissociates from the TfR to bind iron again.<ref>PMID: 16271884</ref><ref>PMID: 6300904</ref>.

<scene name='User:Khaja_Muneeruddin/Sandbox_1/Apotf/2'>Human Transferrin (hTf)</scene>

Molecular Playground banner: A bilobal protein that binds iron and transport it inside the cell.

==3D structures of transferrin==

[[Transferrin]]

==References==
<references/>

User:Jake Pawlowski/Sandbox 1

2014-12-01T16:16:52Z

Jake Pawlowski:

User:Jake Pawlowski/Sandbox 1

2014-12-01T16:15:08Z

Jake Pawlowski:

<Structure load='2HAU' size='500' frame='true' align='right' caption='Human Se-Met transferrin complex with citrate and glycerol [[2hau]]' scene='Insert optional scene name here' />One of the CBI Molecules being studied in the University of Massachusetts Amherst Chemistry-Biology Interface Program at UMass Amherst and on display at the Molecular Playground.

<scene name='User:Khaja_Muneeruddin/Sandbox_1/Apotf/2'>Human Transferrin (hTf)</scene> is a 80 KDa bilobal, iron binding glycoprotein found in blood. In Apo hTf (iron free form), N-lobe (brown) and C-lobe (green) bind one ferric ion each to regulate the concentration of free iron in blood and also transport to iron requiring cells.

N-lobe and C-lobe are homologous and contain identical iron binding amino acid residues. Structurally both N-lobe and C-lobe contain two sub domains namely NI and NII, and CI and CII which come together to form a cleft for binding iron. At the <scene name='User:Khaja_Muneeruddin/Sandbox_1/Nlobe_binding_sites/3'>binding site of N-lobe</scene> Asp63, Tyr188, Tyr95, His249 and Arg124 are involved in trapping of iron<ref>PMID: 9609685</ref>. The amino acids involved in trapping of iron at the <scene name='47/477021/N_lobe_fe_release/3'>binding site</scene> of C-lobe</scene> include Asp392, Tyr426, Tyr517, His585, Arg456<ref>PMID: 15924420</ref>. In addition to these amino acids, at both the lobes a carbonate ion also plays an important role in binding iron. At low pH iron is released from N-lobe by protonation of <scene name='Molecular_Playground/Transferrin/N_lobe_fe_release/2'>Lysines</scene> 206 and 296 <ref>PMID: 9609685</ref> and Lys534 and Arg632 in C-lobe.<ref>PMID: 19917294</ref>

After binding iron N-lobe and C-lobe undergo a conformational change. In ApohTf, N lobe has an <scene name='User:Khaja_Muneeruddin/Sandbox_1/Opennlobe/2'>open conformation</scene> and upon binding ferric ion it shows a <scene name='User:Khaja_Muneeruddin/Sandbox_1/Closed/2'>closed conformation</scene> characterized by rotation of N-II sub domain by 63°<ref>PMID: 9760232</ref>. C-lobe also undergo a similar conformational change upon binding ferric ion, however crystal structure information of the C lobe of hTf is limited due to difficulty in production<ref>PMID: 9337853</ref>.

Intracellular delivery of iron by transferrin is carried out by clathrin-dependent receptor-mediated endocytosis. At pH 7.4 diferric human transferrin binds to human transferrin receptor (hTfR). Upon binding, diferric hTf-hTfR is internalized and in the acidic condition of endosome iron is release from diferric hTf-hTfR complex into the cells. Apo hTf-hTfR complex is recycled back to the cell surface and at pH of cell surface Tf dissociates from the TfR to bind iron again.<ref>PMID: 16271884</ref><ref>PMID: 6300904</ref>.

<scene name='User:Khaja_Muneeruddin/Sandbox_1/Apotf/2'>Human Transferrin (hTf)</scene>

Molecular Playground banner: A bilobal protein that binds iron and transport it inside the cell.

==3D structures of transferrin==

[[Transferrin]]

==References==
<references/>

User:Jake Pawlowski/Sandbox 1

2014-12-01T16:13:47Z

Jake Pawlowski:

<Structure load='2HAU' size='500' frame='true' align='right' caption='Human Se-Met transferrin complex with citrate and glycerol [[2hau]]' scene='Insert optional scene name here' />One of the CBI Molecules being studied in the University of Massachusetts Amherst Chemistry-Biology Interface Program at UMass Amherst and on display at the Molecular Playground.

<scene name='User:Khaja_Muneeruddin/Sandbox_1/Apotf/2'>Human Transferrin (hTf)</scene> is a 80 KDa bilobal, iron binding glycoprotein found in blood. In Apo hTf (iron free form), N-lobe (brown) and C-lobe (green) bind one ferric ion each to regulate the concentration of free iron in blood and also transport to iron requiring cells.

N-lobe and C-lobe are homologous and contain identical iron binding amino acid residues. Structurally both N-lobe and C-lobe contain two sub domains namely NI and NII, and CI and CII which come together to form a cleft for binding iron. At the <scene name='User:Khaja_Muneeruddin/Sandbox_1/Nlobe_binding_sites/3'>binding site of N-lobe</scene> Asp63, Tyr188, Tyr95, His249 and Arg124 are involved in trapping of iron<ref>PMID: 9609685</ref>. The amino acids involved in trapping of iron at the <scene name='47/477021/N_lobe_fe_release/3'>TextToBeDisplayed</scene>binding site of C-lobe</scene> include Asp392, Tyr426, Tyr517, His585, Arg456<ref>PMID: 15924420</ref>. In addition to these amino acids, at both the lobes a carbonate ion also plays an important role in binding iron. At low pH iron is released from N-lobe by protonation of <scene name='Molecular_Playground/Transferrin/N_lobe_fe_release/2'>Lysines</scene> 206 and 296 <ref>PMID: 9609685</ref> and Lys534 and Arg632 in C-lobe.<ref>PMID: 19917294</ref>

After binding iron N-lobe and C-lobe undergo a conformational change. In ApohTf, N lobe has an <scene name='User:Khaja_Muneeruddin/Sandbox_1/Opennlobe/2'>open conformation</scene> and upon binding ferric ion it shows a <scene name='User:Khaja_Muneeruddin/Sandbox_1/Closed/2'>closed conformation</scene> characterized by rotation of N-II sub domain by 63°<ref>PMID: 9760232</ref>. C-lobe also undergo a similar conformational change upon binding ferric ion, however crystal structure information of the C lobe of hTf is limited due to difficulty in production<ref>PMID: 9337853</ref>.

Intracellular delivery of iron by transferrin is carried out by clathrin-dependent receptor-mediated endocytosis. At pH 7.4 diferric human transferrin binds to human transferrin receptor (hTfR). Upon binding, diferric hTf-hTfR is internalized and in the acidic condition of endosome iron is release from diferric hTf-hTfR complex into the cells. Apo hTf-hTfR complex is recycled back to the cell surface and at pH of cell surface Tf dissociates from the TfR to bind iron again.<ref>PMID: 16271884</ref><ref>PMID: 6300904</ref>.

<scene name='User:Khaja_Muneeruddin/Sandbox_1/Apotf/2'>Human Transferrin (hTf)</scene>

Molecular Playground banner: A bilobal protein that binds iron and transport it inside the cell.

==3D structures of transferrin==

[[Transferrin]]

==References==
<references/>

User:Jake Pawlowski/Sandbox 1

2014-12-01T15:43:25Z

Jake Pawlowski:

<Structure load='2HAU' size='500' frame='true' align='right' caption='Human Se-Met transferrin complex with citrate and glycerol [[2hau]]' scene='Insert optional scene name here' />One of the CBI Molecules being studied in the University of Massachusetts Amherst Chemistry-Biology Interface Program at UMass Amherst and on display at the Molecular Playground.

<scene name='User:Khaja_Muneeruddin/Sandbox_1/Apotf/2'>Human Transferrin (hTf)</scene> is a 80 KDa bilobal, iron binding glycoprotein found in blood. In Apo hTf (iron free form), N-lobe (brown) and C-lobe (green) bind one ferric ion each to regulate the concentration of free iron in blood and also transport to iron requiring cells.

N-lobe and C-lobe are homologous and contain identical iron binding amino acid residues. Structurally both N-lobe and C-lobe contain two sub domains namely NI and NII, and CI and CII which come together to form a cleft for binding iron. At the <scene name='User:Khaja_Muneeruddin/Sandbox_1/Nlobe_binding_sites/3'>binding site of N-lobe</scene> Asp63, Tyr188, Tyr95, His249 and Arg124 are involved in trapping of iron<ref>PMID: 9609685</ref>. The amino acids involved in trapping of iron at the <scene name='User:Khaja_Muneeruddin/Sandbox_1/C-lobe_binding_sites/3'>binding site of C-lobe</scene> include Asp392, Tyr426, Tyr517, His585, Arg456<ref>PMID: 15924420</ref>. In addition to these amino acids, at both the lobes a carbonate ion also plays an important role in binding iron. At low pH iron is released from N-lobe by protonation of <scene name='Molecular_Playground/Transferrin/N_lobe_fe_release/2'>Lysines</scene> 206 and 296 <ref>PMID: 9609685</ref> and Lys534 and Arg632 in C-lobe.<ref>PMID: 19917294</ref>

After binding iron N-lobe and C-lobe undergo a conformational change. In ApohTf, N lobe has an <scene name='User:Khaja_Muneeruddin/Sandbox_1/Opennlobe/2'>open conformation</scene> and upon binding ferric ion it shows a <scene name='User:Khaja_Muneeruddin/Sandbox_1/Closed/2'>closed conformation</scene> characterized by rotation of N-II sub domain by 63°<ref>PMID: 9760232</ref>. C-lobe also undergo a similar conformational change upon binding ferric ion, however crystal structure information of the C lobe of hTf is limited due to difficulty in production<ref>PMID: 9337853</ref>.

Intracellular delivery of iron by transferrin is carried out by clathrin-dependent receptor-mediated endocytosis. At pH 7.4 diferric human transferrin binds to human transferrin receptor (hTfR). Upon binding, diferric hTf-hTfR is internalized and in the acidic condition of endosome iron is release from diferric hTf-hTfR complex into the cells. Apo hTf-hTfR complex is recycled back to the cell surface and at pH of cell surface Tf dissociates from the TfR to bind iron again.<ref>PMID: 16271884</ref><ref>PMID: 6300904</ref>.

<scene name='User:Khaja_Muneeruddin/Sandbox_1/Apotf/2'>Human Transferrin (hTf)</scene>

Molecular Playground banner: A bilobal protein that binds iron and transport it inside the cell.

==3D structures of transferrin==

[[Transferrin]]

==References==
<references/>

CBI Molecules

2012-12-13T03:05:59Z

Jake Pawlowski:

These are molecules under study by members of the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program].
Many of the molecules we study are featured at the [http://www.molecularplayground.org/ Molecular Playground] (see also [[Molecular Playground|Molecular Playground in Proteopedia]]). Follow the links below to read nontechnical descriptions, in Proteopedia, of these molecules.

UMass CBI Members, add your molecules to the list (which is alphabetical by CBI research mentor); follow the instructions below the list.

Fall 2012: CBI Molecules are due 12/12/12 and should be added at the TOP of the list from your lab. Label it as "in progress" until you are finished. For those editing an existing CBI Molecule, start from that entry so that it retains the full author list of all authors that contributed (or include credits to the original page and authors if it does not -- I may be able to request additions to the author list).

==Molecules==
'''** Designates CBI Molecules Featured on [http://http://www.umass.edu/cbi/ CBI website]'''

Bhatia Lab

: '''[[Molecular Playground/Alginate-Fall2011]]''', Joe White, David Griffin

: '''[[Molecular Playground/Alginate-Fall2010]]''', Joe White, David Griffin

: '''[[Molecular Playground/Poly(ethylene glycol)]]''', Erika M. Saffer

[http://chamberslab.com/wp/ Chambers Lab]

: '''[[Molecular Playground/Glutamate Receptor]]''', Amanda Hussey, Steve McCarron, Rosie Combs-Bachmann, Mariel Feliciano

[http://openwetware.org/wiki/Chien Chien Lab]

: **'''[[Molecular Playground/Hexameric ClpX]]''', Joanne Lau
:: Best CBI Molecule 2011

: '''[[Molecular Playground/DNA replication initiator DnaA]]''', Jing Liu

Forbes Lab

: '''[[Molecular Playground/CheR]]''', Miaomin Zhang

: '''[[Molecular Playground/RBP]]''', Jan Panteli

: '''[[Molecular Playground/TRAIL]]''', Charley Swofford

[http://www.biochem.umass.edu/garman/index.html Garman Lab]

: '''[[Molecular Playground/Human Protective Protein Cathepsin A]]''', Yadilette Rivera-Colon

: '''[[Molecular Playground/Human PPCA]]''', Nilima Kolli

[http://people.chem.umass.edu/gieraschlab/ Gierasch Lab]

: '''[[CRABP I ( Cellular Retinoic Acid Binding Protein )|Molecular Playground/CRABP I]]''', Kristine Faye Pobre, Mylene Ferrolino,Mangai Periasamy
:: Best Overall CBI Molecule 2010

: '''[[Molecular Playground/CRABP I (Cellular Retinoic Acid Binding Protein)]]''', Gustavo Elberto Epalza Sanchez
(compare this to the previous version above to see what's new)

: **'''[[Molecular_Playground/DHFR]]''', Karan Hingorani
:: Best CBI Molecule 2012

[http://people.chem.umass.edu/jhardy/ Hardy Lab]

: ''' [[Molecular Playground/Caspase-6 and neurodegeneration]]''', Kevin Buadlart Dagbay

: '''[[Molecular Playground/Caspase-7 Dynamics]]'''

: '''[[Molecular Playground/Caspase-9 Regulation]]''', Kristen Huber

: '''[[Molecular Playground/Caspase-6 (new)]]''', Elih Velazquez

: '''[[Molecular Playground/Influenza A M2 transmembrane domain]]''', Samantha Nicholls

: '''[[Molecular Playground/Dengue Virus Protease]]''', Muslum Yildiz

Hebert Lab

: '''[[Molecular_Playground/ERDj5]]''', Lydia Lamriben
: '''[[Molecular Playground/Saposin C]]''', Abla Tannous
: '''[[Molecular_Playground/ERMan1]]''', Johan Sunryd

[http://people.biochem.umass.edu/aheuck/aph.html Heuck Lab]

: '''[[Molecular_Playground/Pcr H]]''', Fabian Romano

[http://www.chem.umass.edu/people/kaltashovlab/ Kaltashov Lab]

: ''' [[Molecular Playground/Transferrin]]''', Khaja Muneeruddin, Jake Pawlowski

: '''[[Molecular Playground/Velaglucerase]]''', Adriana Kita

Knapp lab

:'''[[Molecular Playground/Prolyl Hydroxylase Domain (PHD) Enzyme]]''', Cristina Martin, Serap Pektas
:: Best CBI Molecule Proteopedia Page 2010

: '''[[Molecular Playground/FIH]]''', Cornelius Taabazuing, Breanne Holmes, John Hangasky

[http://people.chem.umass.edu/mmaroney/ Maroney Lab]

: '''[[Molecular Playground/Nickel Superoxide Dismutase]]''', Carolyn Carr
: '''[[Molecular Playground/CsoR and RcnR]]''', Heidi Hu

[http://www.chem.umass.edu/~cmartin/ Martin Lab]

: **'''[[Molecular Playground/T7 RNAP Conformations]]''', Luis E. Ramirez-Tapia
:: Best CBI Molecule 2011
: '''[[Molecular Playground/T7 RNA Polymerase (7 mer int)]]''', Ankit Vahia

: '''[[Molecular Playground/Human mtRNA pol]]''', Ketan Mathavan

Peyton Lab
: '''[[Molecular Playground/C-Raf]]''', Thuy Nguyen
: '''[[Molecular Playground/FAK]]''', Dannielle Ryman

[http://roberts.openwetware.org/ Roberts Lab]

: '''[[Molecular Playground/Taxol]]''', Rohan Patil, Sarah Wilson

: '''[[Molecular Playground/Insulin]]''', Whitney Stoppel

[http://www.umass.edu/rotellogroup/ Rotello Lab]

: '''[[Reverse transcriptase|Molecular Playground/Reverse Transcriptase]]''', Daniel Moyano-Marino

: '''[[Molecular Playground/Pancreatic Lipase]]''', Rui Tang

: '''[[Molecular playground/Chymotrypsin]]''', Brad

: '''[[Molecular Playground/Targeting Peptide]]''', David Solfiell

[https://elements.chem.umass.edu/schnarrlab/ Schnarr Lab ]

: '''[[Molecular Playground/4'-PHOSPHOPANTETHEINYL TRANSFERASE (Sfp)]]''', Jon Amoroso, Gitanjeli Prasad, Lawrence Sheringham Borketey

: '''[[6-deoxyerythronolide_B_synthase_(DEBS)|Molecular Playground/6-Deoxyerythronolide B Synthase]]''', Tsung-Yi Lin, Jon Amoroso

: '''[[Molecular Playground/ACP apo]]''', Gitanjeli Prasad

Tew Lab

: '''[[Molecular Playground/HIV Tat]]''', Brittany deRonde

Thayumanavan Lab

: '''[[Molecular Playground/Lysozyme ]]''', Daniella Gonzalez

: '''[[Molecular Playground/Beta-galactosidase]]''', Judy Ventura

: '''[[User:Krishna Reddy Ragupathi|Molecular Playground/Carbonic Anhydrase]]''', Krishna Reddy Raghupathi

: '''[[User:Rami Rajasekhar Reddy|Molecular Playground/Avidin]]''', Rami Rajasekar Reddy

: '''[[Molecular Playground/Biotin binding avidin]]''', Diego Amado

: '''[[User:Jiaming Zhuang|Molecular Playground/MMP12]]''', Jiaming Zhuang

: ''' [[User:Jing Guo|Molecular Playground/Gluconase]]''', Jing Guo

: '''[[Molecular Playground/Glutathione Reductase]]''', Reuben Chacko

Thayumanavan & Vachet Labs

: '''[[Molecular Playground/Trypsin]]''', Gladys Murage

[http://people.chem.umass.edu/thompson/index.html Thompson] & [http://www.chem.umass.edu/~rmweis/weislab/ Weis] Labs

: '''[[Molecular Playground/Bacterial Chemotaxis Receptors]]''', Lynmarie K. Thompson, Shiela M. Jones

: '''[[Molecular Playground/cytoplasmic domain of a serine chemotaxis receptor]]''', Meili Yang

: '''[[Molecular Playground/Cytoplasmic domain of chemoreceptor of Thermotoga maritima]]''', Xuni Li

[http://www.chem.umass.edu/~vachet/index.html Vachet Lab]

: '''[[Molecular playground/beta 2 microglobulin]]''', Nick Borotto
:: Best CBI Molecule Jmol scenes 2010

: '''[[Molecular Playground/Myoglobin]]''', Yuping Zhou

:'''[[Molecular Playground/ Copper-Zinc Superoxide Dismutase]]''', Shaynah Browne

Other Molecules of interest

: '''[[Molecular Playground/PcrA Helicase]]''', Luis E Ramirez-Tapia, [http://www.chem.umass.edu/~cmartin/ Martin Lab]

Other Laboratories

: '''[[Molecular Playground/YKL-40]]''', Ralph A. Francescone III, [http://www.bio.umass.edu/mcb/faculty/Shao.html Shao Lab]

: '''[[Molecular Playground/BLG|Molecular Playground/β-lactoglobulin]]''', Daniel Seeman, Dubin Lab

: '''[[Molecular Playground/ADAM13]]''', Genevieve Abbruzzese, Alfandari Lab

==Instructions==

'''Congratulations to the prize-winning CBI molecules noted above! The new goal is for students to work collaboratively to create one excellent CBI Molecule for each CBI research group, to be featured on the CBI website.'''

Fall 2012: Complete steps 1-3 by 10/10/12, in preparation for the CBI Molecule Workshop.

1. If you don't already have one, request a Proteopedia account and log in.

2. Get started working in Proteopedia by using the links at [[Help:Contents]]. Make yourself a sandbox page: Enter "User:Your Name/Sandbox 1" (omit quotes) in the search box, then follow instructions to edit this page. Practice entering text, inserting a structure window with scrolling text (green 4-square button on the right), and creating a green scene. You can look at other Proteopedia pages in edit mode to see how different effects (like colored text) are achieved (but this won't show you how the scene effects are made).

3. Get together with the other Chalk Talk students in your research group and decide which molecule you will improve or create. Develop ideas for the scenes you wish to show. You will work on these during the workshop with our help, and then finish them on your own.

You are encouraged to collaborate on this year's CBI Molecules, but everyone will need to do some editing of the molecule so that they each appear as authors on the final list. If you are the sole student from your group enrolled in Chalk Talk and have not previously made a CBI Molecule, try to convince another group member who has previously made a CBI Molecule (see list above) to join us for the workshop so that you can work together.

A successful CBI Molecule will be an interesting, nontechnical description of a molecule related to your group's research. It should not be super long, but instead have multiple green scenes. Green scenes should clearly show an interesting feature and should be attractive. Use the green scenes to help you make interesting points about the molecule (do not try to describe every feature of the molecule). It's great if you can end with a brief statement about how it relates to your group's research goals.

4. Your final pages should be called "Molecular Playground/your molecule" and should have links on this CBI Molecule page -- put the new ones first on the list from your research group. Label them "in progress" until you are finished.

==Links to HELP pages==
Overview at [[Help:Contents ]]

See also [[Help:Getting_Started_in_Proteopedia]]

Videos showing how to use Proteopedia:
[[Proteopedia:Video_Guide]]
(Sometimes slow -- if you pause the video and wait awhile it will download and then you can play it without interruptions)

[[Proteopedia:DIY:Scenes|Proteopedia Scenes: Do It Yourself]]
gives succinct step by step instructions on how to create a molecular scene.

A powerpoint-like set of slides that walks a user through the process of creating a new page and a new molecular scene/green link.
[http://www.proteopedia.org/wiki/images/1/1b/2009_07_13_Proteopedia_Workshop.pdf Proteopedia Workshop Slides]

[[Proteopedia:Guidelines for Ethical Writing]].
Please pay attention to the section about images. There are links to examples of images re-used with explicit permission.

For other help resources, click on [[Help:Contents|Help]] in the ''navigation'' box at the upper left of every page in Proteopedia.

Molecular Playground/Transferrin

2012-12-11T18:40:13Z

Jake Pawlowski:

<Structure load='2HAU' size='500' frame='true' align='right' caption='Human Se-Met transferrin complex with citrate and glycerol [[2hau]]' scene='Insert optional scene name here' />One of the CBI Molecules being studied in the University of Massachusetts Amherst Chemistry-Biology Interface Program at UMass Amherst and on display at the Molecular Playground.

<scene name='User:Khaja_Muneeruddin/Sandbox_1/Apotf/2'>Human Transferrin (hTf)</scene> is a 80 KDa bilobal, iron binding glycoprotein found in blood. In Apo hTf (iron free form), N-lobe (brown) and C-lobe (green) bind one ferric ion each to regulate the concentration of free iron in blood and also transport to iron requiring cells.

N-lobe and C-lobe are homologous and contain identical iron binding amino acid residues. Structurally both N-lobe and C-lobe contain two sub domains namely NI and NII, and CI and CII which come together to form a cleft for binding iron. At the <scene name='User:Khaja_Muneeruddin/Sandbox_1/Nlobe_binding_sites/3'>binding site of N-lobe</scene> Asp63, Tyr188, Tyr95, His249 and Arg124 are involved in trapping of iron<ref>PMID: 9609685</ref>. The amino acids involved in trapping of iron at the <scene name='User:Khaja_Muneeruddin/Sandbox_1/C-lobe_binding_sites/3'>binding site of C-lobe</scene> include Asp392, Tyr426, Tyr517, His585, Arg456<ref>PMID: 15924420</ref>. In addition to these amino acids, at both the lobes a carbonate ion also plays an important role in binding iron.

After binding iron N-lobe and C-lobe undergo a conformational change. In ApohTf, N lobe has an <scene name='User:Khaja_Muneeruddin/Sandbox_1/Opennlobe/2'>open conformation</scene> and upon binding ferric ion it shows a <scene name='User:Khaja_Muneeruddin/Sandbox_1/Closed/2'>closed conformation</scene> characterized by rotation of N-II sub domain by 63°<ref>PMID: 9760232</ref>. C-lobe also undergo a similar conformational change upon binding ferric ion, however crystal structure information of the C lobe of hTf is limited due to difficulty in production<ref>PMID: 9337853</ref>.

Transferrin delivers iron to iron requiring cells by receptor-mediated endocytosis. At basic pH of cell surface diferric human transferrin binds to human transferrin receptor (hTfR). Upon binding, diferric hTf-hTfR is internalized in the cell by endocytosis. In the acidic condition of endosome iron is release from diferric hTf-hTfR complex into the cells. The ApohTf-hTfR complex is recycled back to the cell surface and at the basic pH of cell surface Tf dissociates from the TfR to bind iron again.<ref>PMID: 16271884</ref><ref>PMID: 6300904</ref>.

<scene name='Molecular_Playground/Transferrin/N_lobe_fe_release/2'>Lysines</scene>206 and 296 are protonated at a low pH<ref>PMID: 9609685</ref> which triggers the release of iron.

<scene name='User:Khaja_Muneeruddin/Sandbox_1/Apotf/2'>Human Transferrin (hTf)</scene>

Molecular Playground banner: A bilobal protein that binds iron and transport it inside the cell.

==3D structures of transferrin==

[[Transferrin]]

==References==
<references/>

Molecular Playground/Transferrin

2012-12-11T18:37:44Z

Jake Pawlowski:

<Structure load='2HAU' size='500' frame='true' align='right' caption='Human Se-Met transferrin complex with citrate and glycerol [[2hau]]' scene='Insert optional scene name here' />One of the CBI Molecules being studied in the University of Massachusetts Amherst Chemistry-Biology Interface Program at UMass Amherst and on display at the Molecular Playground.

<scene name='User:Khaja_Muneeruddin/Sandbox_1/Apotf/2'>Human Transferrin (hTf)</scene> is a 80 KDa bilobal, iron binding glycoprotein found in blood. In Apo hTf (iron free form), N-lobe (brown) and C-lobe (green) bind one ferric ion each to regulate the concentration of free iron in blood and also transport to iron requiring cells.

N-lobe and C-lobe are homologous and contain identical iron binding amino acid residues. Structurally both N-lobe and C-lobe contain two sub domains namely NI and NII, and CI and CII which come together to form a cleft for binding iron. At the <scene name='User:Khaja_Muneeruddin/Sandbox_1/Nlobe_binding_sites/3'>binding site of N-lobe</scene> Asp63, Tyr188, Tyr95, His249 and Arg124 are involved in trapping of iron<ref>PMID: 9609685</ref>. The amino acids involved in trapping of iron at the <scene name='User:Khaja_Muneeruddin/Sandbox_1/C-lobe_binding_sites/3'>binding site of C-lobe</scene> include Asp392, Tyr426, Tyr517, His585, Arg456<ref>PMID: 15924420</ref>. In addition to these amino acids, at both the lobes a carbonate ion also plays an important role in binding iron.

After binding iron N-lobe and C-lobe undergo a conformational change. In ApohTf, N lobe has an <scene name='User:Khaja_Muneeruddin/Sandbox_1/Opennlobe/2'>open conformation</scene> and upon binding ferric ion it shows a <scene name='User:Khaja_Muneeruddin/Sandbox_1/Closed/2'>closed conformation</scene> characterized by rotation of N-II sub domain by 63°<ref>PMID: 9760232</ref>. C-lobe also undergo a similar conformational change upon binding ferric ion, however crystal structure information of the C lobe of hTf is limited due to difficulty in production<ref>PMID: 9337853</ref>.

Transferrin delivers iron to iron requiring cells by receptor-mediated endocytosis. At basic pH of cell surface diferric human transferrin binds to human transferrin receptor (hTfR). Upon binding, diferric hTf-hTfR is internalized in the cell by endocytosis. In the acidic condition of endosome iron is release from diferric hTf-hTfR complex into the cells. The ApohTf-hTfR complex is recycled back to the cell surface and at the basic pH of cell surface Tf dissociates from the TfR to bind iron again.<ref>PMID: 16271884</ref><ref>PMID: 6300904</ref>.

<scene name='Molecular_Playground/Transferrin/N_lobe_fe_release/1'>Lysines</scene>206 and 296 are protonated at a low pH<ref>PMID: 9609685</ref> which triggers the release of iron.

<scene name='User:Khaja_Muneeruddin/Sandbox_1/Apotf/2'>Human Transferrin (hTf)</scene>

Molecular Playground banner: A bilobal protein that binds iron and transport it inside the cell.

==3D structures of transferrin==

[[Transferrin]]

==References==
<references/>

Molecular Playground/Transferrin

2012-12-11T18:33:34Z

Jake Pawlowski:

<Structure load='2HAU' size='500' frame='true' align='right' caption='Human Se-Met transferrin complex with citrate and glycerol [[2hau]]' scene='Insert optional scene name here' />One of the CBI Molecules being studied in the University of Massachusetts Amherst Chemistry-Biology Interface Program at UMass Amherst and on display at the Molecular Playground.

<scene name='User:Khaja_Muneeruddin/Sandbox_1/Apotf/2'>Human Transferrin (hTf)</scene> is a 80 KDa bilobal, iron binding glycoprotein found in blood. In Apo hTf (iron free form), N-lobe (brown) and C-lobe (green) bind one ferric ion each to regulate the concentration of free iron in blood and also transport to iron requiring cells.

N-lobe and C-lobe are homologous and contain identical iron binding amino acid residues. Structurally both N-lobe and C-lobe contain two sub domains namely NI and NII, and CI and CII which come together to form a cleft for binding iron. At the <scene name='User:Khaja_Muneeruddin/Sandbox_1/Nlobe_binding_sites/3'>binding site of N-lobe</scene> Asp63, Tyr188, Tyr95, His249 and Arg124 are involved in trapping of iron<ref>PMID: 9609685</ref>. The amino acids involved in trapping of iron at the <scene name='User:Khaja_Muneeruddin/Sandbox_1/C-lobe_binding_sites/3'>binding site of C-lobe</scene> include Asp392, Tyr426, Tyr517, His585, Arg456<ref>PMID: 15924420</ref>. In addition to these amino acids, at both the lobes a carbonate ion also plays an important role in binding iron.

After binding iron N-lobe and C-lobe undergo a conformational change. In ApohTf, N lobe has an <scene name='User:Khaja_Muneeruddin/Sandbox_1/Opennlobe/2'>open conformation</scene> and upon binding ferric ion it shows a <scene name='User:Khaja_Muneeruddin/Sandbox_1/Closed/2'>closed conformation</scene> characterized by rotation of N-II sub domain by 63°<ref>PMID: 9760232</ref>. C-lobe also undergo a similar conformational change upon binding ferric ion, however crystal structure information of the C lobe of hTf is limited due to difficulty in production<ref>PMID: 9337853</ref>.

Transferrin delivers iron to iron requiring cells by receptor-mediated endocytosis. At basic pH of cell surface diferric human transferrin binds to human transferrin receptor (hTfR). Upon binding, diferric hTf-hTfR is internalized in the cell by endocytosis. In the acidic condition of endosome iron is release from diferric hTf-hTfR complex into the cells. The ApohTf-hTfR complex is recycled back to the cell surface and at the basic pH of cell surface Tf dissociates from the TfR to bind iron again.<ref>PMID: 16271884</ref><ref>PMID: 6300904</ref>.

<scene name='Molecular_Playground/Transferrin/N_lobe_fe_release/1'>TextToBeDisplayed</scene>

<scene name='User:Khaja_Muneeruddin/Sandbox_1/Apotf/2'>Human Transferrin (hTf)</scene>

Molecular Playground banner: A bilobal protein that binds iron and transport it inside the cell.

==3D structures of transferrin==

[[Transferrin]]

==References==
<references/>

User:Jake Pawlowski/Sandbox 1

2012-10-10T17:08:27Z

Jake Pawlowski: New page: <Structure load='1AU1' size='500' frame='true' align='right' caption='Insert caption here' scene='Insert optional scene name here' />

User:Jake Pawlowski

2012-10-10T15:09:41Z

Jake Pawlowski:

Jake Pawlowski

Chemistry Graduate Student

University of Massachusetts, Amherst

Amherst, Massachusetts, USA

Pharmacokinetics and detection of post-translational modifications

Bachelors of Science in Chemistry

*[[User:Jake Pawlowski/Sandbox 1]]