1EG4

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

1EG4 の概要

• エントリーDOI: 10.2210/pdb1eg4/pdb
• 関連するPDBエントリー: 1EG3
• 分子名称: BETA-DYSTROGLYCAN, DYSTROPHIN (3 entities in total)
• 機能のキーワード: ef-hand like domain, ww domain, polyproline type ii (ppii) helix, structural protein
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Alpha-dystroglycan: Secreted, extracellular space. Beta-dystroglycan: Cell membrane; Single- pass type I membrane protein: Q14118; Cell membrane, sarcolemma; Peripheral membrane protein; Cytoplasmic side: P11532
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 31591.27

構造登録者

Huang, X.,Poy, F.,Zhang, R.,Joachimiak, A.,Sudol, M.,Eck, M.J. (登録日: 2000-02-11, 公開日: 2000-08-23, 最終更新日: 2024-02-07)

主引用文献

Huang, X.,Poy, F.,Zhang, R.,Joachimiak, A.,Sudol, M.,Eck, M.J.
Structure of a WW domain containing fragment of dystrophin in complex with beta-dystroglycan.
Nat.Struct.Biol., 7:634-638, 2000

PubMed Abstract: 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.

PubMed: 10932245
DOI: 10.1038/77923

実験手法

X-RAY DIFFRACTION (2 Å)