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1anw

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Revision as of 10:32, 15 November 2017

THE EFFECT OF METAL BINDING ON THE STRUCTURE OF ANNEXIN V AND IMPLICATIONS FOR MEMBRANE BINDING

Structural highlights

1anw is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

[ANXA5_HUMAN] Defects in ANXA5 are associated with susceptibility to pregnancy loss, recurrent, type 3 (RPRGL3) [MIM:614391]. A common complication of pregnancy, resulting in spontaneous abortion before the fetus has reached viability. The term includes all miscarriages from the time of conception until 24 weeks of gestation. Recurrent pregnancy loss is defined as 3 or more consecutive spontaneous abortions.^[1]

Function

[ANXA5_HUMAN] 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 PubMed

The structure of annexin V, crystallised in the presence of two calcium or barium ions for each protein molecule, was solved by molecular replacement to 0.24 nm resolution. The two metal ions are found in domains I and IV, i.e. on the same side of the channel that lies in the centre of the molecule. The structures of the barium and calcium form are extremely close, the only differences localised in the metal-binding sites that lie on the surface of the molecule. The occupancies of the metal ions, however, are lower for barium than for calcium, expressing the lower affinity of the protein for the former. The packing of the annexin molecules in the crystal asymmetric unit may represent a model for the calcium driven association of membrane-bound annexins that leads to membrane fusion.

The effect of metal binding on the structure of annexin V and implications for membrane binding.,Lewit-Bentley A, Morera S, Huber R, Bodo G Eur J Biochem. 1992 Nov 15;210(1):73-7. PMID:1446685^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Bogdanova N, Horst J, Chlystun M, Croucher PJ, Nebel A, Bohring A, Todorova A, Schreiber S, Gerke V, Krawczak M, Markoff A. A common haplotype of the annexin A5 (ANXA5) gene promoter is associated with recurrent pregnancy loss. Hum Mol Genet. 2007 Mar 1;16(5):573-8. Epub 2007 Mar 5. PMID:17339269 doi:10.1093/hmg/ddm017
↑ Lewit-Bentley A, Morera S, Huber R, Bodo G. The effect of metal binding on the structure of annexin V and implications for membrane binding. Eur J Biochem. 1992 Nov 15;210(1):73-7. PMID:1446685

1 Structural highlights
2 Disease
3 Function
4 Evolutionary Conservation
5 Publication Abstract from PubMed
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1anw"

@@ Line 1: / Line 1: @@
 ==THE EFFECT OF METAL BINDING ON THE STRUCTURE OF ANNEXIN V AND IMPLICATIONS FOR MEMBRANE BINDING==
 <StructureSection load='1anw' size='340' side='right' caption='[[1anw]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
@@ Line 4: / Line 5: @@
 <table><tr><td colspan='2'>[[1anw]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ANW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ANW FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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=1anw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1anw OCA], [http://pdbe.org/1anw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1anw RCSB], [http://www.ebi.ac.uk/pdbsum/1anw PDBsum]</span></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=1anw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1anw OCA], [http://pdbe.org/1anw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1anw RCSB], [http://www.ebi.ac.uk/pdbsum/1anw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1anw ProSAT]</span></td></tr>
 </table>
 == Disease ==
@@ Line 29: / Line 30: @@
 </div>
 <div class="pdbe-citations 1anw" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Annexin|Annexin]]
 == References ==
 <references/>

1anw

From Proteopedia

Revision as of 10:32, 15 November 2017

THE EFFECT OF METAL BINDING ON THE STRUCTURE OF ANNEXIN V AND IMPLICATIONS FOR MEMBRANE BINDING

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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