9D58

Human Dystrophin tandem calponin homology actin-binding domain crystallized in a closed-state conformation

9D58 の概要

• エントリーDOI: 10.2210/pdb9d58/pdb
• 分子名称: Dystrophin (2 entities in total)
• 機能のキーワード: actin-binding domain, tandem calponin homology domain, dystrophin, duchenne muscular dystrophy, dmd, cytoskeleton, structural protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 114293.25

構造登録者

Streeter, O.,Shi, K.,Ervasti, J.M.,Evans III, R.L.,Muretta, J.M. (登録日: 2024-08-13, 公開日: 2025-03-12)

主引用文献

Streeter, O.,Shi, K.,Vavra, J.,Aihara, H.,Ervasti, J.M.,Evans 3rd, R.,Muretta, J.M.
Human dystrophin tandem calponin homology actin-binding domain crystallized in a closed-state conformation.
Acta Crystallogr D Struct Biol, 81:122-129, 2025

PubMed Abstract: The structure of the N-terminal actin-binding domain of human dystrophin was determined at 1.94 Å resolution. Each chain in the asymmetric unit exists in a `closed' conformation, with the first and second calponin homology (CH) domains directly interacting via a 2500.6 Å interface. The positioning of the individual CH domains is comparable to the domain-swapped dimer seen in previous human dystrophin and utrophin actin-binding domain 1 structures. The CH1 domain is highly similar to the actin-bound utrophin structure and structural homology suggests that the `closed' single-chain conformation opens during actin binding to mitigate steric clashes between CH2 and actin.

PubMed: 40007458
DOI: 10.1107/S2059798325001457

実験手法

X-RAY DIFFRACTION (1.94 Å)