1aii
From Proteopedia
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(New page: 200px<br /> <applet load="1aii" size="450" color="white" frame="true" align="right" spinBox="true" caption="1aii, resolution 1.95Å" /> '''ANNEXIN III'''<br /...)
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Revision as of 15:59, 29 October 2007
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ANNEXIN III
Overview
Annexin III, a putative inositol (1,2)-phosphohydrolase, was, co-crystallized with inositol 2-phosphate, the inhibitor of the reaction, and its structure was solved to 1.95 A resolution. No enzyme active site, was observed in the structure. Assays for enzymatic activity were also, negative. Search for annexin III-inositol phosphate interactions using the, BIAcoreTM system revealed an affinity for inositol cyclic (1,2)-phosphate, suggesting annexin III may sequester the molecule in the cell. The, BIAcoreTM system used with different phospholipids showed that annexin III, displays specificity for phosphatidylethanolamine, but not for, phosphatidylinositols. Interestingly, a molecule of ethanolamine was found, bound to the protein in the crystal structure. Coupled with the fact that, this is ... [(full description)]
About this Structure
1AII is a [Single protein] structure of sequence from [Homo sapiens] with CA, SO4 and ETA as [ligands]. Full crystallographic information is available from [OCA].
Reference
Can enzymatic activity, or otherwise, be inferred from structural studies of annexin III?, Perron B, Lewit-Bentley A, Geny B, Russo-Marie F, J Biol Chem. 1997 Apr 25;272(17):11321-6. PMID:9111038
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