1u2c
From Proteopedia
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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 Wed Nov 21 03:47:38 2007
