This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
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 Tue Oct 30 | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:48:43 2007'' |
Revision as of 12:44, 30 October 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 ... [(full description)]
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 Tue Oct 30 14:48:43 2007
