1h67
From Proteopedia
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| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h67 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h67 OCA], [http://www.ebi.ac.uk/pdbsum/1h67 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1h67 RCSB]</span> | ||
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[[Category: nmr]] | [[Category: nmr]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:58:40 2008'' |
Revision as of 17:58, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NMR STRUCTURE OF THE CH DOMAIN OF CALPONIN
Overview
Calponin 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.
About this Structure
1H67 is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
Reference
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
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