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1wyn
From Proteopedia
(Difference between revisions)
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<StructureSection load='1wyn' size='340' side='right'caption='[[1wyn]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | <StructureSection load='1wyn' size='340' side='right'caption='[[1wyn]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1wyn]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[1wyn]] 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=1WYN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WYN FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CNN2 ([ | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CNN2 ([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=1wyn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wyn OCA], [https://pdbe.org/1wyn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wyn RCSB], [https://www.ebi.ac.uk/pdbsum/1wyn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wyn ProSAT], [https://www.topsan.org/Proteins/RSGI/1wyn TOPSAN]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://www.uniprot.org/uniprot/CNN2_HUMAN CNN2_HUMAN]] Thin filament-associated protein that is implicated in the regulation and modulation of smooth muscle contraction. It is capable of binding to actin, calmodulin, troponin C and tropomyosin. The interaction of calponin with actin inhibits the actomyosin Mg-ATPase activity. |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 07:01, 2 March 2022
Solution structure of the CH domain of human calponin-2
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