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< | ==RAT ANNEXIN V COMPLEXED WITH GLYCEROPHOSPHOETHANOLAMINE== | ||
<StructureSection load='1a8b' size='340' side='right'caption='[[1a8b]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1a8b]] 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=1A8B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1A8B FirstGlance]. <br> | |||
</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='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=GPE:L-ALPHA-GLYCEROPHOSPHORYLETHANOLAMINE'>GPE</scene></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=1a8b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a8b OCA], [https://pdbe.org/1a8b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1a8b RCSB], [https://www.ebi.ac.uk/pdbsum/1a8b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1a8b ProSAT]</span></td></tr> | |||
</table> | |||
== 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 == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/a8/1a8b_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</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/main_output.php?pdb_ID=1a8b ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Structural 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<ref>PMID:7583670</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1a8b" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Annexin 3D structures|Annexin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
== | |||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Concha NO]] | |||
[[Category: Concha | [[Category: Dedman JR]] | ||
[[Category: Dedman | [[Category: Kaetzel MA]] | ||
[[Category: Kaetzel | [[Category: Seaton BA]] | ||
[[Category: Seaton | [[Category: Swairjo MA]] | ||
[[Category: Swairjo | |||
Latest revision as of 10:15, 23 October 2024
RAT ANNEXIN V COMPLEXED WITH GLYCEROPHOSPHOETHANOLAMINERAT ANNEXIN V COMPLEXED WITH GLYCEROPHOSPHOETHANOLAMINE
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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