2dmh: Difference between revisions
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==Solution structure of the first C2 domain of human myoferlin== | |||
<StructureSection load='2dmh' size='340' side='right'caption='[[2dmh]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2dmh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DMH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2DMH FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2dmh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dmh OCA], [https://pdbe.org/2dmh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2dmh RCSB], [https://www.ebi.ac.uk/pdbsum/2dmh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2dmh ProSAT], [https://www.topsan.org/Proteins/RSGI/2dmh TOPSAN]</span></td></tr> | ||
[[2dmh]] is a 1 chain structure with sequence from [ | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/MYOF_HUMAN MYOF_HUMAN] Calcium/phospholipid-binding protein that plays a role in the plasmalemma repair mechanism of endothelial cells that permits rapid resealing of membranes disrupted by mechanical stress. Involved in endocytic recycling. Implicated in VEGF signal transduction by regulating the levels of the receptor KDR (By similarity). | |||
== 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/dm/2dmh_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=2dmh ConSurf]. | |||
<div style="clear:both"></div> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Hayashi F]] | ||
[[Category: | [[Category: Nagashima T]] | ||
[[Category: Yokoyama | [[Category: Yokoyama S]] | ||
Latest revision as of 21:44, 29 May 2024
Solution structure of the first C2 domain of human myoferlinSolution structure of the first C2 domain of human myoferlin
Structural highlights
FunctionMYOF_HUMAN Calcium/phospholipid-binding protein that plays a role in the plasmalemma repair mechanism of endothelial cells that permits rapid resealing of membranes disrupted by mechanical stress. Involved in endocytic recycling. Implicated in VEGF signal transduction by regulating the levels of the receptor KDR (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. |
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