3ZY7

Crystal structure of computationally redesigned gamma-adaptin appendage domain forming a symmetric homodimer

3ZY7 の概要

• エントリーDOI: 10.2210/pdb3zy7/pdb
• 関連するPDBエントリー: 1GYU 1GYV 1GYW 1W63 2A7B
• 分子名称: AP-1 COMPLEX SUBUNIT GAMMA-1, ISOPROPYL ALCOHOL, DI(HYDROXYETHYL)ETHER, ... (4 entities in total)
• 機能のキーワード: endocytosis, protein design, computational design
• 由来する生物種: MUS MUSCULUS (HOUSE MOUSE)
• 細胞内の位置: Golgi apparatus: P22892
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 27607.30

構造登録者

Stranges, P.B.,Machius, M.,Miley, M.J.,Tripathy, A.,Kuhlman, B. (登録日: 2011-08-17, 公開日: 2011-12-28, 最終更新日: 2023-12-20)

主引用文献

Stranges, P.B.,Machius, M.,Miley, M.J.,Tripathy, A.,Kuhlman, B.
Computational Design of a Symmetric Homodimer Using Beta-Strand Assembly.
Proc.Natl.Acad.Sci.USA, 108:20562-, 2011

PubMed Abstract: Computational design of novel protein-protein interfaces is a test of our understanding of protein interactions and has the potential to allow modification of cellular physiology. Methods for designing high-affinity interactions that adopt a predetermined binding mode have proved elusive, suggesting the need for new strategies that simplify the design process. A solvent-exposed backbone on a β-strand is thought of as "sticky" and β-strand pairing stabilizes many naturally occurring protein complexes. Here, we computationally redesign a monomeric protein to form a symmetric homodimer by pairing exposed β-strands to form an intermolecular β-sheet. A crystal structure of the designed complex closely matches the computational model (rmsd = 1.0 Å). This work demonstrates that β-strand pairing can be used to computationally design new interactions with high accuracy.

PubMed: 22143762
DOI: 10.1073/PNAS.1115124108

実験手法

X-RAY DIFFRACTION (1.09 Å)