2dmh: Difference between revisions

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==Solution structure of the first C2 domain of human myoferlin==
==Solution structure of the first C2 domain of human myoferlin==
<StructureSection load='2dmh' size='340' side='right' caption='[[2dmh]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
<StructureSection load='2dmh' size='340' side='right' caption='[[2dmh]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<table><tr><td colspan='2'>[[2dmh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DMH FirstGlance]. <br>
<table><tr><td colspan='2'>[[2dmh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2DMH FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FER1L3, KIAA1207, MYOF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FER1L3, KIAA1207, MYOF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2dmh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dmh OCA], [http://pdbe.org/2dmh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2dmh RCSB], [http://www.ebi.ac.uk/pdbsum/2dmh PDBsum], [http://www.topsan.org/Proteins/RSGI/2dmh TOPSAN]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2dmh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2dmh OCA], [http://pdbe.org/2dmh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2dmh RCSB], [http://www.ebi.ac.uk/pdbsum/2dmh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2dmh ProSAT], [http://www.topsan.org/Proteins/RSGI/2dmh TOPSAN]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dm/2dmh_consurf.spt"</scriptWhenChecked>
     <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>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>

Revision as of 09:56, 30 May 2018

Solution structure of the first C2 domain of human myoferlinSolution structure of the first C2 domain of human myoferlin

Structural highlights

2dmh is a 1 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:FER1L3, KIAA1207, MYOF (HUMAN)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

Function

[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

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA