3PZD

Structure of the myosin X MyTH4-FERM/DCC complex

3PZD の概要

• エントリーDOI: 10.2210/pdb3pzd/pdb
• 分子名称: Myosin-X, Netrin receptor DCC, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: protein-protein complex, myth4 domain, ferm domain, cargo binding, motor protein-apoptosis complex, motor protein/apoptosis
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm, cytosol: Q9HD67; Membrane; Single-pass type I membrane protein: P70211
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 62700.61

構造登録者

Wei, Z.,Yan, J.,Pan, L.,Zhang, M. (登録日: 2010-12-14, 公開日: 2011-02-23, 最終更新日: 2024-03-20)

主引用文献

Wei, Z.,Yan, J.,Lu, Q.,Pan, L.,Zhang, M.
Cargo recognition mechanism of myosin X revealed by the structure of its tail MyTH4-FERM tandem in complex with the DCC P3 domain
Proc.Natl.Acad.Sci.USA, 108:3572-3577, 2011

PubMed Abstract: Myosin X (MyoX), encoded by Myo10, is a representative member of the MyTH4-FERM domain-containing myosins, and this family of unconventional myosins shares common functions in promoting formation of filopodia/stereocilia structures in many cell types with unknown mechanisms. Here, we present the structure of the MyoX MyTH4-FERM tandem in complex with the cytoplasmic tail P3 domain of the netrin receptor DCC. The structure, together with biochemical studies, reveals that the MyoX MyTH4 and FERM domains interact with each other, forming a structural and functional supramodule. Instead of forming an extended β-strand structure in other FERM binding targets, DCC_P3 forms a single α-helix and binds to the αβ-groove formed by β5 and α1 of the MyoX FERM F3 lobe. Structure-based amino acid sequence analysis reveals that the key polar residues forming the inter-MyTH4/FERM interface are absolutely conserved in all MyTH4-FERM tandem-containing proteins, suggesting that the supramodular nature of the MyTH4-FERM tandem is likely a general property for all MyTH4-FERM proteins.

PubMed: 21321230
DOI: 10.1073/pnas.1016567108

実験手法

X-RAY DIFFRACTION (2.5 Å)