3cdz

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{{STRUCTURE_3cdz| PDB=3cdz | SCENE= }}
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==Crystal structure of human factor VIII==
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===Crystal structure of human factor VIII===
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<StructureSection load='3cdz' size='340' side='right' caption='[[3cdz]], [[Resolution|resolution]] 3.98&Aring;' scene=''>
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{{ABSTRACT_PUBMED_18400180}}
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3cdz]] is a 2 chain structure with 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=3CDZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3CDZ FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene><br>
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<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">F8, F8C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3cdz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3cdz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3cdz RCSB], [http://www.ebi.ac.uk/pdbsum/3cdz PDBsum]</span></td></tr>
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<table>
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== Disease ==
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[[http://www.uniprot.org/uniprot/FA8_HUMAN FA8_HUMAN]] Defects in F8 are the cause of hemophilia A (HEMA) [MIM:[http://omim.org/entry/306700 306700]]. A disorder of blood coagulation characterized by a permanent tendency to hemorrhage. About 50% of patients have severe hemophilia resulting in frequent spontaneous bleeding into joints, muscles and internal organs. Less severe forms are characterized by bleeding after trauma or surgery. Note=Of particular interest for the understanding of the function of F8 is the category of CRM (cross-reacting material) positive patients (approximately 5%) that have considerable amount of F8 in their plasma (at least 30% of normal), but the protein is non-functional; i.e. the F8 activity is much less than the plasma protein level. CRM-reduced is another category of patients in which the F8C antigen and activity are reduced to approximately the same level. Most mutations are CRM negative, and probably affect the folding and stability of the protein.<ref>PMID:3012775</ref> <ref>PMID:3122181</ref> <ref>PMID:2833855</ref> <ref>PMID:2835904</ref> <ref>PMID:2499363</ref> <ref>PMID:2506948</ref> <ref>PMID:2510835</ref> <ref>PMID:2495245</ref> <ref>PMID:2498882</ref> <ref>PMID:2104766</ref> <ref>PMID:2105106</ref> <ref>PMID:1973901</ref> <ref>PMID:2105906</ref> <ref>PMID:2106480</ref> <ref>PMID:2107542</ref> <ref>PMID:1908817</ref> <ref>PMID:1908096</ref> <ref>PMID:1851341</ref> <ref>PMID:1356412</ref> <ref>PMID:1639429</ref> <ref>PMID:1349567</ref> <ref>PMID:1301194</ref> <ref>PMID:1301932</ref> <ref>PMID:1301960</ref> <ref>PMID:8449505</ref> <ref>PMID:8322269</ref> <ref>PMID:7579394</ref> <ref>PMID:7794769</ref> <ref>PMID:7759074</ref> <ref>PMID:8644728</ref> <ref>PMID:8639447</ref> <ref>PMID:8759905</ref> <ref>PMID:9029040</ref> <ref>PMID:9326186</ref> <ref>PMID:9341862</ref> <ref>PMID:9886318</ref> <ref>PMID:9450898</ref> <ref>PMID:10215414</ref> <ref>PMID:9603440</ref> <ref>PMID:9452104</ref> <ref>PMID:9792405</ref> <ref>PMID:9829908</ref> <ref>PMID:9569180</ref> <ref>PMID:9569189</ref> <ref>PMID:10554831</ref> <ref>PMID:10338101</ref> <ref>PMID:10408784</ref> <ref>PMID:10404764</ref> <ref>PMID:10910910</ref> <ref>PMID:10910913</ref> <ref>PMID:10691849</ref> <ref>PMID:10886198</ref> <ref>PMID:10800171</ref> <ref>PMID:10896236</ref> <ref>PMID:10612839</ref> <ref>PMID:11410838</ref> <ref>PMID:11298607</ref> <ref>PMID:11442643</ref> <ref>PMID:11442647</ref> <ref>PMID:11554935</ref> <ref>PMID:11748850</ref> <ref>PMID:11341489</ref> <ref>PMID:12351418</ref> <ref>PMID:12406074</ref> <ref>PMID:12199686</ref> <ref>PMID:11857744</ref> <ref>PMID:12203998</ref> <ref>PMID:12325022</ref> <ref>PMID:11858487</ref> <ref>PMID:12195713</ref> <ref>PMID:12930394</ref> <ref>PMID:12871415</ref> <ref>PMID:12614369</ref> <ref>PMID:15682412</ref> <ref>PMID:15810915</ref> <ref>PMID:16805874</ref> <ref>PMID:18184865</ref> <ref>PMID:21371196</ref>
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== Function ==
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[[http://www.uniprot.org/uniprot/FA8_HUMAN FA8_HUMAN]] Factor VIII, along with calcium and phospholipid, acts as a cofactor for factor IXa when it converts factor X to the activated form, factor Xa.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cd/3cdz_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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/chain_selection.php?pdb_ID=2ata ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Factor VIII is a procofactor that plays a critical role in blood coagulation, and is missing or defective in hemophilia A. We determined the X-ray crystal structure of B domain-deleted human factor VIII. This protein is composed of five globular domains and contains one Ca(2+) and two Cu(2+) ions. The three homologous A domains form a triangular heterotrimer where the A1 and A3 domains serve as the base and interact with the C2 and C1 domains, respectively. The structurally homologous C1 and C2 domains reveal membrane binding features. Based on biochemical studies, a model of the factor IXa-factor VIIIa complex was constructed by in silico docking. Factor IXa wraps across the side of factor VIII, and an extended interface spans the factor VIII heavy and light chains. This model provides insight into the activation of factor VIII and the interaction of factor VIIIa with factor IXa on the membrane surface.
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==Disease==
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Crystal structure of human factor VIII: implications for the formation of the factor IXa-factor VIIIa complex.,Ngo JC, Huang M, Roth DA, Furie BC, Furie B Structure. 2008 Apr;16(4):597-606. PMID:18400180<ref>PMID:18400180</ref>
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[[http://www.uniprot.org/uniprot/FA8_HUMAN FA8_HUMAN]] Defects in F8 are the cause of hemophilia A (HEMA) [MIM:[http://omim.org/entry/306700 306700]]. A disorder of blood coagulation characterized by a permanent tendency to hemorrhage. About 50% of patients have severe hemophilia resulting in frequent spontaneous bleeding into joints, muscles and internal organs. Less severe forms are characterized by bleeding after trauma or surgery. Note=Of particular interest for the understanding of the function of F8 is the category of CRM (cross-reacting material) positive patients (approximately 5%) that have considerable amount of F8 in their plasma (at least 30% of normal), but the protein is non-functional; i.e. the F8 activity is much less than the plasma protein level. CRM-reduced is another category of patients in which the F8C antigen and activity are reduced to approximately the same level. Most mutations are CRM negative, and probably affect the folding and stability of the protein.<ref>PMID:3012775</ref><ref>PMID:3122181</ref><ref>PMID:2833855</ref><ref>PMID:2835904</ref><ref>PMID:2499363</ref><ref>PMID:2506948</ref><ref>PMID:2510835</ref><ref>PMID:2495245</ref><ref>PMID:2498882</ref><ref>PMID:2104766</ref><ref>PMID:2105106</ref><ref>PMID:1973901</ref><ref>PMID:2105906</ref><ref>PMID:2106480</ref><ref>PMID:2107542</ref><ref>PMID:1908817</ref><ref>PMID:1908096</ref><ref>PMID:1851341</ref><ref>PMID:1356412</ref><ref>PMID:1639429</ref><ref>PMID:1349567</ref><ref>PMID:1301194</ref><ref>PMID:1301932</ref><ref>PMID:1301960</ref><ref>PMID:8449505</ref><ref>PMID:8322269</ref><ref>PMID:7579394</ref><ref>PMID:7794769</ref><ref>PMID:7759074</ref><ref>PMID:8644728</ref><ref>PMID:8639447</ref><ref>PMID:8759905</ref><ref>PMID:9029040</ref><ref>PMID:9326186</ref><ref>PMID:9341862</ref><ref>PMID:9886318</ref><ref>PMID:9450898</ref><ref>PMID:10215414</ref><ref>PMID:9603440</ref><ref>PMID:9452104</ref><ref>PMID:9792405</ref><ref>PMID:9829908</ref><ref>PMID:9569180</ref><ref>PMID:9569189</ref><ref>PMID:10554831</ref><ref>PMID:10338101</ref><ref>PMID:10408784</ref><ref>PMID:10404764</ref><ref>PMID:10910910</ref><ref>PMID:10910913</ref><ref>PMID:10691849</ref><ref>PMID:10886198</ref><ref>PMID:10800171</ref><ref>PMID:10896236</ref><ref>PMID:10612839</ref><ref>PMID:11410838</ref><ref>PMID:11298607</ref><ref>PMID:11442643</ref><ref>PMID:11442647</ref><ref>PMID:11554935</ref><ref>PMID:11748850</ref><ref>PMID:11341489</ref><ref>PMID:12351418</ref><ref>PMID:12406074</ref><ref>PMID:12199686</ref><ref>PMID:11857744</ref><ref>PMID:12203998</ref><ref>PMID:12325022</ref><ref>PMID:11858487</ref><ref>PMID:12195713</ref><ref>PMID:12930394</ref><ref>PMID:12871415</ref><ref>PMID:12614369</ref><ref>PMID:15682412</ref><ref>PMID:15810915</ref><ref>PMID:16805874</ref><ref>PMID:18184865</ref><ref>PMID:21371196</ref>
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==Function==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[http://www.uniprot.org/uniprot/FA8_HUMAN FA8_HUMAN]] Factor VIII, along with calcium and phospholipid, acts as a cofactor for factor IXa when it converts factor X to the activated form, factor Xa.
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</div>
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==About this Structure==
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[[3cdz]] is a 2 chain structure with 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=3CDZ OCA].
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==See Also==
==See Also==
*[[Factor VIII|Factor VIII]]
*[[Factor VIII|Factor VIII]]
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== References ==
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==Reference==
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<references/>
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<ref group="xtra">PMID:018400180</ref><references group="xtra"/><references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Furie, B.]]
[[Category: Furie, B.]]

Revision as of 21:01, 2 October 2014

Crystal structure of human factor VIII

3cdz, resolution 3.98Å

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