2d88
From Proteopedia
(Difference between revisions)
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==Solution structure of the CH domain from human MICAL-3 protein== | ==Solution structure of the CH domain from human MICAL-3 protein== | ||
| - | <StructureSection load='2d88' size='340' side='right' caption='[[2d88]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2d88' size='340' side='right'caption='[[2d88]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2d88]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2d88]] 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=2D88 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2D88 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MICAL3 ([ | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MICAL3 ([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=2d88 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d88 OCA], [https://pdbe.org/2d88 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2d88 RCSB], [https://www.ebi.ac.uk/pdbsum/2d88 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2d88 ProSAT], [https://www.topsan.org/Proteins/RSGI/2d88 TOPSAN]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/MICA3_HUMAN MICA3_HUMAN]] Monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin. Acts by modifying actin subunits through the addition of oxygen to form methionine-sulfoxide, leading to promote actin filament severing and prevent repolymerization (By similarity). Involved in exocytic vesicles tethering and fusion: the monooxygenase activity is required for this process.<ref>PMID:21596566</ref> |
== 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: Inoue, M]] | [[Category: Inoue, M]] | ||
[[Category: Kigawa, T]] | [[Category: Kigawa, T]] | ||
Revision as of 11:55, 3 February 2021
Solution structure of the CH domain from human MICAL-3 protein
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