1fv4

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{{Theoretical_model}}
{{Theoretical_model}}
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{{Seed}}
 
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[[Image:1fv4.png|left|200px]]
 
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==THREE DIMENSIONAL MODEL OF COAGULATION FACTOR VA==
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The line below this paragraph, containing "STRUCTURE_1fv4", creates the "Structure Box" on the page.
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<StructureSection load='1fv4' size='340' side='right'caption='[[1fv4]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FV4 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fv4 FirstGlance], [https://www.ebi.ac.uk/pdbsum/1fv4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fv4 ProSAT]</span></td></tr>
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</table>
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{{STRUCTURE_1fv4| PDB=1fv4 | SCENE= }}
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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A complete molecular model of blood coagulation factor Va (FVa) bound to anticoagulant activated protein C (APC) and to a phospholipid membrane was constructed. The three homologous A domains and the two homologous C domains of FVA were modeled based on the X-ray crystallographic structures of ceruloplasmin and C2 domain of factor V, respectively. The final arrangement of the five domains in the complete FVa model bound to a membrane incorporated extensive published experimental data. FVa binds the phospholipid membrane through its C2 domain while the A-domain trimer is located from 40 through 100 A above the membrane plane. From our model we infer a probable role for metal ions at the interface between FVa light and heavy chains, provide an explanation for the slower APC cleavage at Arg306 relative to Arg506, and predict specific interactions between positively and negatively charged exosites in APC and FVa, respectively.
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===THREE DIMENSIONAL MODEL OF COAGULATION FACTOR VA===
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Three-dimensional model of coagulation factor Va bound to activated protein C.,Pellequer JL, Gale AJ, Getzoff ED, Griffin JH Thromb Haemost. 2000 Nov;84(5):849-57. PMID:11127867<ref>PMID:11127867</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_11127867}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 1fv4" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 11127867 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_11127867}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Theoretical Model]]
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Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FV4 OCA].
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[[Category: Large Structures]]
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==Reference==
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<ref group="xtra">PMID:11127867</ref><references group="xtra"/>
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[[Category: Pellequer, J.-L]]
[[Category: Pellequer, J.-L]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Apr 8 08:07:54 2010''
 

Current revision

Theoretical Model: The protein structure described on this page was determined theoretically, and hence should be interpreted with caution.

THREE DIMENSIONAL MODEL OF COAGULATION FACTOR VA

PDB ID 1fv4

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