1H67: NMR Structure of the CH Domain of Calponin

Citation:
Abstract
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.
PDB ID: 1H67Download
MMDB ID: 18703
PDB Deposition Date: 2001/6/7
Updated in MMDB: 2007/11
Experimental Method:
solution nmr
Source Organism:
Similar Structures:
Biological Unit for 1H67: monomeric; determined by author
Molecular Components in 1H67
Label Count Molecule
Protein (1 molecule)
1
Calponin Alpha
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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