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| | <StructureSection load='1kig' size='340' side='right'caption='[[1kig]], [[Resolution|resolution]] 3.00Å' scene=''> | | <StructureSection load='1kig' size='340' side='right'caption='[[1kig]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1kig]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Argasid_tick Argasid tick] and [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KIG OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KIG FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1kig]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Ornithodoros_moubata Ornithodoros moubata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KIG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KIG FirstGlance]. <br> |
| - | </td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Coagulation_factor_Xa Coagulation factor Xa], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.6 3.4.21.6] </span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kig OCA], [http://pdbe.org/1kig PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kig RCSB], [http://www.ebi.ac.uk/pdbsum/1kig PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kig ProSAT]</span></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=1kig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kig OCA], [https://pdbe.org/1kig PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kig RCSB], [https://www.ebi.ac.uk/pdbsum/1kig PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kig ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FA10_BOVIN FA10_BOVIN]] Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting. [[http://www.uniprot.org/uniprot/TAP_ORNMO TAP_ORNMO]] TAP is a slow, tight-binding inhibitor of blood coagulation, specific for factor Xa. | + | [https://www.uniprot.org/uniprot/FA10_BOVIN FA10_BOVIN] Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ki/1kig_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ki/1kig_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Argasid tick]] | + | [[Category: Bos taurus]] |
| - | [[Category: Bovin]]
| + | |
| - | [[Category: Coagulation factor Xa]]
| + | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Alexander, R]] | + | [[Category: Ornithodoros moubata]] |
| - | [[Category: Chang, C H]] | + | [[Category: Alexander R]] |
| - | [[Category: Wei, A]] | + | [[Category: Chang C-H]] |
| - | [[Category: Blood coagulation]]
| + | [[Category: Wei A]] |
| - | [[Category: Glycoprotein]]
| + | |
| - | [[Category: Plasma]]
| + | |
| - | [[Category: Serine protease]]
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| Structural highlights
Function
FA10_BOVIN Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The structure of recombinant tick anticoagulant peptide (rTAP) complexed to bovine factor Xa at 3.0 A resolution reveals the structural basis for the specificity and the high affinity of rTAP. Three N-terminal residues, Tyr501, Asn502 and Arg503, play a critical role in the complex formation as suggested by earlier mutagenic studies and the ornithodorin-thrombin complex. Unexpectedly, the side-chain of Tyr501 is located in the S1 pocket, although factor Xa favors arginine as a P1 residue. Arg503 is located at the aryl binding pocket and forms a salt-bridge with Glu97 of factor Xa. The autolysis loop, which is disordered in the uninhibited factor Xa structure, is involved in the formation of the complex as a part of the secondary binding site. The C-terminal helix of rTAP interacts with factor Xa as a secondary binding determinant. The N-terminal residues of rTAP reorganize during the formation of the factor Xa-rTAP complex from the conformation found in the solution into an extended conformation. The presence of the secondary binding site confirms the proposed two-step kinetic mechanism based on the results of a mutagenesis study.
Unexpected binding mode of tick anticoagulant peptide complexed to bovine factor Xa.,Wei A, Alexander RS, Duke J, Ross H, Rosenfeld SA, Chang CH J Mol Biol. 1998;283(1):147-54. PMID:9761680[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wei A, Alexander RS, Duke J, Ross H, Rosenfeld SA, Chang CH. Unexpected binding mode of tick anticoagulant peptide complexed to bovine factor Xa. J Mol Biol. 1998;283(1):147-54. PMID:9761680 doi:10.1006/jmbi.1998.2069
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