1BHD

SECOND CALPONIN HOMOLOGY DOMAIN FROM UTROPHIN

Summary for 1BHD

• Entry DOI: 10.2210/pdb1bhd/pdb
• Descriptor: UTROPHIN (2 entities in total)
• Functional Keywords: calponin homology, actin binding, structural protein
• Biological source: Homo sapiens (human)
• Cellular location: Cell junction, synapse, postsynaptic cell membrane; Peripheral membrane protein; Cytoplasmic side: P46939
• Total number of polymer chains: 2
• Total formula weight: 27357.36

Authors

Keep, N.H.,Winder, S.J.,Kendrick-Jones, J. (deposition date: 1998-06-05, release date: 1999-01-13, Last modification date: 2024-05-22)

Primary citation

Keep, N.H.,Norwood, F.L.,Moores, C.A.,Winder, S.J.,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., 285:1257-1264, 1999

PubMed 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 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.

PubMed: 9887274
DOI: 10.1006/jmbi.1998.2406

Experimental method

X-RAY DIFFRACTION (2 Å)