1U2C

Crystal Structure of a-dystroglycan

1U2C の概要

• エントリーDOI: 10.2210/pdb1u2c/pdb
• 分子名称: Dystroglycan (2 entities in total)
• 機能のキーワード: ig-like domain, s6 like fold, protein binding
• 由来する生物種: Mus musculus (house mouse)
• 細胞内の位置: Alpha-dystroglycan: Secreted, extracellular space (By similarity). Beta-dystroglycan: Cell membrane; Single- pass type I membrane protein (By similarity): Q62165
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 26226.78

構造登録者

Bozic, D.,Sciandra, F.,Lamba, D.,Brancaccio, A. (登録日: 2004-07-18, 公開日: 2004-09-07, 最終更新日: 2024-11-13)

主引用文献

Bozic, D.,Sciandra, F.,Lamba, D.,Brancaccio, A.
The Structure of the N-terminal Region of Murine Skeletal Muscle {alpha}-Dystroglycan Discloses a Modular Architecture
J.Biol.Chem., 279:44812-44816, 2004

PubMed Abstract: 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.

PubMed: 15326183
DOI: 10.1074/jbc.C400353200

実験手法

X-RAY DIFFRACTION (2.3 Å)