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=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2dmh]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2dmh]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/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 ([ | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FER1L3, KIAA1207, MYOF ([https://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'>[ | <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> | ||
</table> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
[[Category: Large Structures]] | |||
[[Category: Hayashi, F]] | [[Category: Hayashi, F]] | ||
[[Category: Nagashima, T]] | [[Category: Nagashima, T]] | ||
Revision as of 15:08, 3 February 2021
Solution structure of the first C2 domain of human myoferlinSolution structure of the first C2 domain of human myoferlin
Structural highlights
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. |
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