1h67: Difference between revisions
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==NMR Structure of the CH Domain of Calponin== | ==NMR Structure of the CH Domain of Calponin== | ||
<StructureSection load='1h67' size='340' side='right'caption='[[1h67 | <StructureSection load='1h67' size='340' side='right'caption='[[1h67]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1h67]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1h67]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H67 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H67 FirstGlance]. <br> | ||
</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=1h67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h67 OCA], [https://pdbe.org/1h67 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h67 RCSB], [https://www.ebi.ac.uk/pdbsum/1h67 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h67 ProSAT]</span></td></tr> | </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=1h67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h67 OCA], [https://pdbe.org/1h67 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h67 RCSB], [https://www.ebi.ac.uk/pdbsum/1h67 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h67 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/CNN1_CHICK CNN1_CHICK] 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]] | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Gallus gallus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Barlow | [[Category: Barlow PN]] | ||
[[Category: Bramham | [[Category: Bramham J]] | ||
[[Category: Smith | [[Category: Smith BO]] | ||
[[Category: Uhrin | [[Category: Uhrin D]] | ||
[[Category: Winder | [[Category: Winder SJ]] | ||
Latest revision as of 08:30, 15 May 2024
NMR Structure of the CH Domain of CalponinNMR Structure of the CH Domain of Calponin
Structural highlights
FunctionCNN1_CHICK 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 Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCalponin is involved in the regulation of contractility and organization of the actin cytoskeleton in smooth muscle cells. It is the archetypal member of the calponin homology (CH) domain family of actin binding proteins that includes cytoskeletal linkers such as alpha-actinin, spectrin, and dystrophin, and regulatory proteins including VAV, IQGAP, and calponin. We have determined the first structure of a CH domain from a single CH domain-containing protein, that of calponin, and have fitted the NMR-derived coordinates to the 3D-helical reconstruction of the F-actin:calponin complex using cryo-electron microscopy. The tertiary fold of this single CH domain is typical of, yet significantly different from, those of the CH domains that occur in tandem pairs to form high-affinity ABDs in other proteins. We thus provide a structural insight into the mode of interaction between F-actin and CH domain-containing proteins. Solution structure of the calponin CH domain and fitting to the 3D-helical reconstruction of F-actin:calponin.,Bramham J, Hodgkinson JL, Smith BO, Uhrin D, Barlow PN, Winder SJ Structure. 2002 Feb;10(2):249-58. PMID:11839310[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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