Structural highlights
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 PubMed
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 A 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.
The 2.0 A structure of the second calponin homology domain from the actin-binding region of the dystrophin homologue utrophin.,Keep NH, Norwood FL, Moores CA, Winder SJ, Kendrick-Jones J J Mol Biol. 1999 Jan 22;285(3):1257-64. PMID:9887274[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Keep NH, Norwood FL, Moores CA, Winder SJ, Kendrick-Jones J. The 2.0 A structure of the second calponin homology domain from the actin-binding region of the dystrophin homologue utrophin. J Mol Biol. 1999 Jan 22;285(3):1257-64. PMID:9887274 doi:10.1006/jmbi.1998.2406
