1aii
From Proteopedia
| Line 23: | Line 23: | ||
[[Category: phospholipase a2 inhibitor]] | [[Category: phospholipase a2 inhibitor]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 15:48:23 2007'' |
Revision as of 13:43, 5 November 2007
|
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
Page seeded by OCA on Mon Nov 5 15:48:23 2007
