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1aii
From Proteopedia
(Difference between revisions)
(New page: 200px<br /> <applet load="1aii" size="450" color="white" frame="true" align="right" spinBox="true" caption="1aii, resolution 1.95Å" /> '''ANNEXIN III'''<br /...) |
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| - | [[Image:1aii.gif|left|200px]]<br /> | ||
| - | <applet load="1aii" size="450" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1aii, resolution 1.95Å" /> | ||
| - | '''ANNEXIN III'''<br /> | ||
| - | == | + | ==ANNEXIN III== |
| - | Annexin III, a putative inositol (1,2)-phosphohydrolase, was | + | <StructureSection load='1aii' size='340' side='right'caption='[[1aii]], [[Resolution|resolution]] 1.95Å' scene=''> |
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1aii]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AII OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AII FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ETA:ETHANOLAMINE'>ETA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1aii FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aii OCA], [https://pdbe.org/1aii PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aii RCSB], [https://www.ebi.ac.uk/pdbsum/1aii PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aii ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ANXA3_HUMAN ANXA3_HUMAN] Inhibitor of phospholipase A2, also possesses anti-coagulant properties. Also cleaves the cyclic bond of inositol 1,2-cyclic phosphate to form inositol 1-phosphate. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ai/1aii_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1aii ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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. | ||
| - | + | 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<ref>PMID:9111038</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1aii" style="background-color:#fffaf0;"></div> | |
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| - | + | ==See Also== | |
| + | *[[Annexin 3D structures|Annexin 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Lewit-Bentley A]] | ||
| + | [[Category: Perron B]] | ||
Current revision
ANNEXIN III
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