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1a8b: Difference between revisions

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== Structural highlights ==
== 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>
<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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GPE:L-ALPHA-GLYCEROPHOSPHORYLETHANOLAMINE'>GPE</scene></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]] 1.9&#8491;</td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene></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>
<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>
</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.  
[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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</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].
</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].
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== 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1a8b" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Annexin 3D structures|Annexin 3D structures]]
*[[Annexin 3D structures|Annexin 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Concha, N O]]
[[Category: Concha NO]]
[[Category: Dedman, J R]]
[[Category: Dedman JR]]
[[Category: Kaetzel, M A]]
[[Category: Kaetzel MA]]
[[Category: Seaton, B A]]
[[Category: Seaton BA]]
[[Category: Swairjo, M A]]
[[Category: Swairjo MA]]
[[Category: Calcium binding protein]]
[[Category: Membrane binding protein]]
[[Category: Phospholipid analog]]

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