1H67

NMR Structure of the CH Domain of Calponin

Summary for 1H67

• Entry DOI: 10.2210/pdb1h67/pdb
• NMR Information: BMRB: 4880
• Descriptor: CALPONIN ALPHA (1 entity in total)
• Functional Keywords: cytoskeleton, calponin homology domain, actin binding
• Biological source: GALLUS GALLUS (CHICKEN)
• Total number of polymer chains: 1
• Total formula weight: 12266.95

Authors

Bramham, J.,Smith, B.O.,Uhrin, D.,Barlow, P.N.,Winder, S.J. (deposition date: 2001-06-07, release date: 2002-02-14, Last modification date: 2024-05-15)

Primary citation

Bramham, J.,Hodgkinson, J.L.,Smith, B.O.,Uhrin, D.,Barlow, P.N.,Winder, S.J.
Solution Structure of the Calponin Ch Domain and Fitting to the 3D-Helical Reconstruction of F-Actin:Calponin.
Structure, 10:249-, 2002

PubMed 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.

PubMed: 11839310
DOI: 10.1016/S0969-2126(02)00703-7

Experimental method

SOLUTION NMR