1bhd

SECOND CALPONIN HOMOLOGY DOMAIN FROM UTROPHIN

spinqualitylabelsall models 1bhd, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1bhd is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function UTRN_HUMAN May play a role in anchoring the cytoskeleton to the plasma membrane. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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