1aii
From Proteopedia
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|PDB= 1aii |SIZE=350|CAPTION= <scene name='initialview01'>1aii</scene>, resolution 1.95Å | |PDB= 1aii |SIZE=350|CAPTION= <scene name='initialview01'>1aii</scene>, resolution 1.95Å | ||
|SITE= <scene name='pdbsite=CAD:Secondary+Ca+Binding+Site+In+Domain+Iii'>CAD</scene>, <scene name='pdbsite=CBD:Secondary+Ca+Binding+Site+In+Domain+Iii'>CBD</scene> and <scene name='pdbsite=CCD:Secondary+Ca+Binding+Site+In+Domain+Iii'>CCD</scene> | |SITE= <scene name='pdbsite=CAD:Secondary+Ca+Binding+Site+In+Domain+Iii'>CAD</scene>, <scene name='pdbsite=CBD:Secondary+Ca+Binding+Site+In+Domain+Iii'>CBD</scene> and <scene name='pdbsite=CCD:Secondary+Ca+Binding+Site+In+Domain+Iii'>CCD</scene> | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ETA:ETHANOLAMINE'>ETA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1aii FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aii OCA], [http://www.ebi.ac.uk/pdbsum/1aii PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1aii RCSB]</span> | ||
}} | }} | ||
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[[Category: Lewit-Bentley, A.]] | [[Category: Lewit-Bentley, A.]] | ||
[[Category: Perron, B.]] | [[Category: Perron, B.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: ETA]] | ||
| - | [[Category: SO4]] | ||
[[Category: annexin]] | [[Category: annexin]] | ||
[[Category: calcium/phospholipid binding protein]] | [[Category: calcium/phospholipid binding protein]] | ||
[[Category: phospholipase a2 inhibitor]] | [[Category: phospholipase a2 inhibitor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:40:59 2008'' |
Revision as of 15:41, 30 March 2008
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| , resolution 1.95Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | , and | ||||||
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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