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1anx

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Revision as of 18:09, 14 August 2019

THE CRYSTAL STRUCTURE OF A NEW HIGH-CALCIUM FORM OF ANNEXIN V

Structural highlights

1anx is a 3 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

Annexin V was crystallized in the presence of a high concentration of calcium and the structure refined at 1.9 A resolution. The crystals are triclinic (P1) with three molecules per asymmetric unit and pseudo-R3 symmetry, reflecting a tendency of annexin to form trimers. The overall structure of the protein is similar to that seen in other crystal forms. There are, however, significant changes in domain III, where a new calcium site is formed. The whole region surrounding this site is reorganized in our structure, rendering annexin V more symmetrical and more alike annexin I. The formation of the new calcium site causes the displacement of Trp187 from a buried to an exposed conformation, a change that has recently been demonstrated by fluorescence measurements. The affinity of the different potential calcium sites is modulated: there is no calcium bound in domains II and IV, while up to two secondary calcium ions sites (in domains I and III) can substitute, depending on the calcium concentration present. We suggest that annexin can act as a calcium buffer, binding or releasing calcium depending on its local concentration. Our results also show that annexin displays inherent mobility which, together with its capacity to modulate the calcium affinity of its sites, can be of importance for its function on the membrane surface.

The crystal structure of a new high-calcium form of annexin V.,Sopkova J, Renouard M, Lewit-Bentley A J Mol Biol. 1993 Dec 5;234(3):816-25. PMID:8254674^[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
↑ Sopkova J, Renouard M, Lewit-Bentley A. The crystal structure of a new high-calcium form of annexin V. J Mol Biol. 1993 Dec 5;234(3):816-25. PMID:8254674 doi:http://dx.doi.org/10.1006/jmbi.1993.1627

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
 ==THE CRYSTAL STRUCTURE OF A NEW HIGH-CALCIUM FORM OF ANNEXIN V==
-<StructureSection load='1anx' size='340' side='right' caption='[[1anx]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+<StructureSection load='1anx' size='340' side='right'caption='[[1anx]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1anx]] is a 3 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=1ANX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ANX FirstGlance]. <br>
@@ Line 15: / Line 15: @@
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/an/1anx_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/an/1anx_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
@@ Line 30: / Line 30: @@
 </div>
 <div class="pdbe-citations 1anx" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Annexin 3D structures|Annexin 3D structures]]
 == References ==
 <references/>
@@ Line 35: / Line 38: @@
 </StructureSection>
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Lewit-Bentley, A]]
 [[Category: Renouard, M]]

1anx

From Proteopedia

Revision as of 18:09, 14 August 2019

THE CRYSTAL STRUCTURE OF A NEW HIGH-CALCIUM FORM OF ANNEXIN V

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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