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1eg4

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1eg4, resolution 2.00Å ()
Domains: efhand_1, WW, efhand_2
Related: 1eg3
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



STRUCTURE OF A DYSTROPHIN WW DOMAIN FRAGMENT IN COMPLEX WITH A BETA-DYSTROGLYCAN PEPTIDE

Publication Abstract from PubMed

Dystrophin and beta-dystroglycan are components of the dystrophin-glycoprotein complex (DGC), a multimolecular assembly that spans the cell membrane and links the actin cytoskeleton to the extracellular basal lamina. Defects in the dystrophin gene are the cause of Duchenne and Becker muscular dystrophies. The C-terminal region of dystrophin binds the cytoplasmic tail of beta-dystroglycan, in part through the interaction of its WW domain with a proline-rich motif in the tail of beta-dystroglycan. Here we report the crystal structure of this portion of dystrophin in complex with the proline-rich binding site in beta-dystroglycan. The structure shows that the dystrophin WW domain is embedded in an adjacent helical region that contains two EF-hand-like domains. The beta-dystroglycan peptide binds a composite surface formed by the WW domain and one of these EF-hands. Additionally, the structure reveals striking similarities in the mechanisms of proline recognition employed by WW domains and SH3 domains.

Structure of a WW domain containing fragment of dystrophin in complex with beta-dystroglycan., Huang X, Poy F, Zhang R, Joachimiak A, Sudol M, Eck MJ, Nat Struct Biol. 2000 Aug;7(8):634-8. PMID:10932245

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1EG4 is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

  • Huang X, Poy F, Zhang R, Joachimiak A, Sudol M, Eck MJ. Structure of a WW domain containing fragment of dystrophin in complex with beta-dystroglycan. Nat Struct Biol. 2000 Aug;7(8):634-8. PMID:10932245 doi:10.1038/77923

Page seeded by OCA on Wed Feb 18 02:32:10 2009

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