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[[Image:1anw.gif|left|200px]]


{{Structure
==THE EFFECT OF METAL BINDING ON THE STRUCTURE OF ANNEXIN V AND IMPLICATIONS FOR MEMBRANE BINDING==
|PDB= 1anw |SIZE=350|CAPTION= <scene name='initialview01'>1anw</scene>, resolution 2.40&Aring;
<StructureSection load='1anw' size='340' side='right'caption='[[1anw]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
<table><tr><td colspan='2'>[[1anw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1ANW FirstGlance]. <br>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
|GENE=  
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=1anw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1anw OCA], [https://pdbe.org/1anw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1anw RCSB], [https://www.ebi.ac.uk/pdbsum/1anw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1anw ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/ANXA5_HUMAN ANXA5_HUMAN] Defects in ANXA5 are associated with susceptibility to pregnancy loss, recurrent, type 3 (RPRGL3) [MIM:[https://omim.org/entry/614391 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.<ref>PMID:17339269</ref>  
== Function ==
[https://www.uniprot.org/uniprot/ANXA5_HUMAN 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 ==
[[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/an/1anw_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1anw ConSurf].
<div style="clear:both"></div>


'''THE EFFECT OF METAL BINDING ON THE STRUCTURE OF ANNEXIN V AND IMPLICATIONS FOR MEMBRANE BINDING'''
==See Also==
 
*[[Annexin 3D structures|Annexin 3D structures]]
 
== References ==
==Overview==
<references/>
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.
__TOC__
 
</StructureSection>
==About this Structure==
1ANW is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ANW OCA].
 
==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/1446685 1446685]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Bodo, G.]]
[[Category: Bodo G]]
[[Category: Huber, R.]]
[[Category: Huber R]]
[[Category: Lewit-Bentley, A.]]
[[Category: Lewit-Bentley A]]
[[Category: Morera, S.]]
[[Category: Morera S]]
[[Category: CA]]
[[Category: calcium/phospholipid-binding protein]]
 
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