1aii: Difference between revisions
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==Overview== | ==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 . | 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 a particularly abundant phospholipid in granules specific to, neutrophils, cells where annexin III is highly expressed, our finding, could be pointing to a physiological role of annexin III. | ||
==About this Structure== | ==About this Structure== | ||
1AII is a | 1AII is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA, SO4 and ETA as [http://en.wikipedia.org/wiki/ligands ligands]. Structure known Active Sites: CAD, CBD and CCD. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AII OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: phospholipase a2 inhibitor]] | [[Category: phospholipase a2 inhibitor]] | ||
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Revision as of 11:14, 5 November 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 a particularly abundant phospholipid in granules specific to, neutrophils, cells where annexin III is highly expressed, our finding, could be pointing to a physiological role of annexin III.
About this Structure
1AII is a Single protein structure of sequence from Homo sapiens with CA, SO4 and ETA as ligands. Structure known Active Sites: CAD, CBD and CCD. 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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