1m9i

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[[Image:1m9i.jpg|left|200px]]
 
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{{Structure
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==Crystal Structure Of Phosphorylation-Mimicking Mutant T356D Of Annexin VI==
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|PDB= 1m9i |SIZE=350|CAPTION= <scene name='initialview01'>1m9i</scene>, resolution 2.65&Aring;
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<StructureSection load='1m9i' size='340' side='right'caption='[[1m9i]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
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<table><tr><td colspan='2'>[[1m9i]] 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=1M9I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M9I 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]] 2.65&#8491;</td></tr>
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|GENE= ANX6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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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></td></tr>
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}}
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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=1m9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m9i OCA], [https://pdbe.org/1m9i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m9i RCSB], [https://www.ebi.ac.uk/pdbsum/1m9i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m9i ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ANXA6_HUMAN ANXA6_HUMAN] May associate with CD21. May regulate the release of Ca(2+) from intracellular stores.
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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/m9/1m9i_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=1m9i ConSurf].
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<div style="clear:both"></div>
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'''Crystal Structure Of Phosphorylation-Mimicking Mutant T356D Of Annexin VI'''
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==See Also==
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*[[Annexin 3D structures|Annexin 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Phosphorylation of some members of the annexin family of proteins may play a significant role in controlling their calcium-dependent interactions with membranes. Recent electron microscopic studies of annexin VI revealed that the protein's two core domains exhibit a great degree of flexibility and are able to undergo a relative conformational change that could potentially initiate contacts between membranes [Avila-Sakar, A. J., et al. (2000) J. Struct. Biol. 130, 54-62]. To assess the possibility of a regulatory role of phosphorylation in this behavior, the crystal structure of a phosphorylation-mimicking mutant (T356D in the flexible connector region of human annexin VI) was determined to 2.65 A resolution. When the mutant is compared to the wild-type annexin VI, subtle differences are seen at the site of the mutation, while larger changes are evident in one of the calcium-binding loops and in the presence of five calcium ions. Furthermore, biochemical studies provide evidence for additional conformational differences between the T356D and wild-type solution structures. Fluorescence emission and acrylamide quenching suggest a higher level of solvent exposure of Trp-343 in the connector region of T356D in the presence of calcium. Comparisons of retardation coefficients in native gel electrophoresis reveal that T356D has a more extended shape, while proteolytic studies show a greater accessibility of a trypsin cleavage site inside the linker region, indicating a conformation more open than the wild-type form. These data provide insights into a possible regulatory mechanism leading to a higher degree of flexibility and possibly a higher calcium binding affinity of annexin VI upon phosphorylation.
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==About this Structure==
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1M9I 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=1M9I OCA].
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==Reference==
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Structural and dynamic changes in human annexin VI induced by a phosphorylation-mimicking mutation, T356D., Freye-Minks C, Kretsinger RH, Creutz CE, Biochemistry. 2003 Jan 28;42(3):620-30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12534274 12534274]
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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: Creutz, C E.]]
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[[Category: Creutz CE]]
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[[Category: Freye-Minks, C.]]
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[[Category: Freye-Minks C]]
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[[Category: Kretsinger, R H.]]
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[[Category: Kretsinger RH]]
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[[Category: CA]]
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[[Category: annexin]]
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[[Category: calcium-binding]]
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[[Category: membrane-binding]]
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[[Category: mutant t356d]]
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[[Category: phosphorylation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:40:41 2008''
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Current revision

Crystal Structure Of Phosphorylation-Mimicking Mutant T356D Of Annexin VI

PDB ID 1m9i

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