1a8a: Difference between revisions
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<StructureSection load='1a8a' size='340' side='right'caption='[[1a8a]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='1a8a' size='340' side='right'caption='[[1a8a]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1a8a]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1a8a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A8A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A8A FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GSE:L-ALPHA-GLYCEROPHOSPHORYLSERINE'>GSE</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1a8a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a8a OCA], [https://pdbe.org/1a8a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a8a RCSB], [https://www.ebi.ac.uk/pdbsum/1a8a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a8a ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/ANXA5_RAT ANXA5_RAT] This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Concha | [[Category: Concha NO]] | ||
[[Category: Dedman | [[Category: Dedman JR]] | ||
[[Category: Kaetzel | [[Category: Kaetzel MA]] | ||
[[Category: Seaton | [[Category: Seaton BA]] | ||
[[Category: Swairjo | [[Category: Swairjo MA]] | ||
Latest revision as of 10:45, 15 November 2023
RAT ANNEXIN V COMPLEXED WITH GLYCEROPHOSPHOSERINERAT ANNEXIN V COMPLEXED WITH GLYCEROPHOSPHOSERINE
Structural highlights
FunctionANXA5_RAT This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade. 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 PubMedStructural evidence is presented for a 'Ca(2+)-bridging' mechanism, proposed for Ca(2+)-binding interfacial membrane proteins such as annexins, protein kinase C, and certain coagulation proteins. Crystal structures of Ca(2+)-annexin V complexes with phospholipid polar heads provide molecular details of 'Ca(2+)-bridges' as key features in the membrane attachment exhibited by these proteins. Distinct binding sites for phospholipid head groups are observed, including a novel, double-Ca2+ recognition site for phosphoserine that may serve as a phosphatidylserine receptor site in vivo. Ca(2+)-bridging mechanism and phospholipid head group recognition in the membrane-binding protein annexin V.,Swairjo MA, Concha NO, Kaetzel MA, Dedman JR, Seaton BA Nat Struct Biol. 1995 Nov;2(11):968-74. PMID:7583670[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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