1aii
From Proteopedia
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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 , and as ligands. Known structural/functional Sites: , and . 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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