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New page: left|200px<br /> <applet load="1m9i" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m9i, resolution 2.65Å" /> '''Crystal Structure O...
 
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[[Image:1m9i.gif|left|200px]]<br />
<applet load="1m9i" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1m9i, resolution 2.65&Aring;" />
'''Crystal Structure Of Phosphorylation-Mimicking Mutant T356D Of Annexin VI'''<br />


==Overview==
==Crystal Structure Of Phosphorylation-Mimicking Mutant T356D Of Annexin VI==
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.
<StructureSection load='1m9i' size='340' side='right'caption='[[1m9i]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
<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>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ANXA6_HUMAN ANXA6_HUMAN] May associate with CD21. May regulate the release of Ca(2+) from intracellular stores.
== 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/m9/1m9i_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=1m9i ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1M9I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M9I OCA].
*[[Annexin 3D structures|Annexin 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=12534274 12534274]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Creutz, C.E.]]
[[Category: Creutz CE]]
[[Category: Freye-Minks, C.]]
[[Category: Freye-Minks C]]
[[Category: Kretsinger, R.H.]]
[[Category: Kretsinger RH]]
[[Category: CA]]
[[Category: annexin]]
[[Category: calcium-binding]]
[[Category: membrane-binding]]
[[Category: mutant t356d]]
[[Category: phosphorylation]]
 
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