1AII
ANNEXIN III
Summary for 1AII
| Entry DOI | 10.2210/pdb1aii/pdb |
| Descriptor | ANNEXIN III, CALCIUM ION, SULFATE ION, ... (5 entities in total) |
| Functional Keywords | calcium/phospholipid binding protein, annexin, phospholipase a2 inhibitor, calcium-phospholipid binding protein complex |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 36784.81 |
| Authors | Lewit-Bentley, A.,Perron, B. (deposition date: 1996-11-28, release date: 1997-03-12, Last modification date: 2023-11-15) |
| Primary citation | Perron, B.,Lewit-Bentley, A.,Geny, B.,Russo-Marie, F. Can enzymatic activity, or otherwise, be inferred from structural studies of annexin III? J.Biol.Chem., 272:11321-11326, 1997 Cited by PubMed Abstract: 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. PubMed: 9111038DOI: 10.1074/jbc.272.17.11321 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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