1aii

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[[Image:1aii.gif|left|200px]]
 
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{{Structure
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==ANNEXIN III==
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|PDB= 1aii |SIZE=350|CAPTION= <scene name='initialview01'>1aii</scene>, resolution 1.95&Aring;
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<StructureSection load='1aii' size='340' side='right'caption='[[1aii]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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|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>
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ETA:ETHANOLAMINE'>ETA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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<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>
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|ACTIVITY=
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
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|GENE=
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<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>
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|DOMAIN=
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<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>
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|RELATEDENTRY=
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</table>
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|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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== Function ==
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}}
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[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.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ai/1aii_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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'''ANNEXIN III'''
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1aii" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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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.
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*[[Annexin 3D structures|Annexin 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1AII is a [[Single protein]] structure of sequence from [http://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].
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__TOC__
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</StructureSection>
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==Reference==
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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:[http://www.ncbi.nlm.nih.gov/pubmed/9111038 9111038]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Lewit-Bentley, A.]]
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[[Category: Lewit-Bentley A]]
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[[Category: Perron, B.]]
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[[Category: Perron B]]
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[[Category: annexin]]
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[[Category: calcium/phospholipid binding protein]]
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[[Category: phospholipase a2 inhibitor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:40:59 2008''
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Current revision

ANNEXIN III

PDB ID 1aii

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