1u2c
From Proteopedia
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'''Crystal Structure of a-dystroglycan''' | '''Crystal Structure of a-dystroglycan''' | ||
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[[Category: Lamba, D.]] | [[Category: Lamba, D.]] | ||
[[Category: Sciandra, F.]] | [[Category: Sciandra, F.]] | ||
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Revision as of 07:40, 3 May 2008
Crystal Structure of a-dystroglycan
Overview
Dystroglycan (DG) is a cell surface receptor consisting of two subunits: alpha-dystroglycan, extracellular and highly glycosylated, and beta-dystroglycan, spanning the cell membrane. It is a pivotal member of the dystrophin-glycoprotein complex and is involved in a wide variety of important cellular processes such as the stabilization of the muscle fiber sarcolemma or the clustering of acetylcholine receptors. We report the 2.3-A resolution crystal structure of the murine skeletal muscle N-terminal alpha-DG region, which confirms the presence of two autonomous domains; the first finally identified as an Ig-like and the second resembling ribosomal RNA-binding proteins. Solid-phase laminin binding assays show the occurrence of protein-protein type of interactions involving the Ig-like domain of alpha-DG.
About this Structure
1U2C is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
The structure of the N-terminal region of murine skeletal muscle alpha-dystroglycan discloses a modular architecture., Bozic D, Sciandra F, Lamba D, Brancaccio A, J Biol Chem. 2004 Oct 22;279(43):44812-6. Epub 2004 Aug 23. PMID:15326183 Page seeded by OCA on Sat May 3 10:40:12 2008
