1anx: Difference between revisions
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[[Image:1anx.gif|left|200px]] | [[Image:1anx.gif|left|200px]] | ||
'''THE CRYSTAL STRUCTURE OF A NEW HIGH-CALCIUM FORM OF ANNEXIN V''' | {{Structure | ||
|PDB= 1anx |SIZE=350|CAPTION= <scene name='initialview01'>1anx</scene>, resolution 1.90Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''THE CRYSTAL STRUCTURE OF A NEW HIGH-CALCIUM FORM OF ANNEXIN V''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1ANX is a [ | 1ANX 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=1ANX OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8254674 8254674] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: calcium/phospholipid-binding protein]] | [[Category: calcium/phospholipid-binding protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:00:06 2008'' | ||
Revision as of 11:00, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE CRYSTAL STRUCTURE OF A NEW HIGH-CALCIUM FORM OF ANNEXIN V
OverviewOverview
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.
About this StructureAbout this Structure
1ANX is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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
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