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The 2.0 angstrom structure of the second calponin homology domain from the actin-binding region of the dystrophin homologue utrophin

Keep, NH; Norwood, FLM; Moores, CA; Winder, SJ; Kendrick-Jones, J; (1999) The 2.0 angstrom structure of the second calponin homology domain from the actin-binding region of the dystrophin homologue utrophin. J MOL BIOL , 285 (3) 1257 - 1264.

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Abstract

Utrophin is a close homologue of dystrophin, the protein defective in Duchenne muscular dystrophy. Like dystrophin, it is composed of three regions: an N-terminal region that binds actin filaments, a large central region with triple coiled-coil repeats, and a C-terminal region that interacts with components in the dystroglycan protein complex at the plasma membrane. The N-terminal actin-binding region consists of two calponin homology domains and is related to the actin-binding domains of a superfamily of proteins including alpha-actinin, spectrin and fimbrin. Here, we present the 2.0 Angstrom structure of the second calponin homology domain of utrophin solved by X-ray crystallography, and compare it to the other calponin homology domains previously determined from spectrin and fimbrin. (C) 1999 Academic Press.

Type:Article
Title:The 2.0 angstrom structure of the second calponin homology domain from the actin-binding region of the dystrophin homologue utrophin
Keywords:utrophin, dystrophin, actin, calponin, crystal structure, F-ACTIN, ALPHA-ACTININ, TERMINAL REGION, DEFICIENT MICE, PROTEIN MODELS, SEQUENCE, REFINEMENT, MUSCLE, IDENTIFICATION, GLYCOPROTEIN
UCL classification:UCL > School of Life and Medical Sciences > Faculty of Life Sciences > Biosciences (Division of)

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