2JT4

Solution Structure of the Sla1 SH3-3-Ubiquitin Complex

2JT4 の概要

• エントリーDOI: 10.2210/pdb2jt4/pdb
• 関連するPDBエントリー: 1UBQ 1Z9Z
• 分子名称: Cytoskeleton assembly control protein SLA1, Ubiquitin (2 entities in total)
• 機能のキーワード: endocytosis, monoubiquitin signaling, ubiquitin-binding motif, sh3, ubiquitin, actin-binding, cytoplasm, cytoskeleton, phosphorylation, sh3 domain, dna damage, dna repair, nucleus, ubl conjugation, signaling protein
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast); 詳細
• 細胞内の位置: Nucleus: P32790
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 16748.15

構造登録者

He, Y.,Radhakrishnan, I. (登録日: 2007-07-18, 公開日: 2007-09-25, 最終更新日: 2024-05-29)

主引用文献

He, Y.,Hicke, L.,Radhakrishnan, I.
Structural Basis for Ubiquitin Recognition by SH3 Domains
J.Mol.Biol., 373:190-196, 2007

PubMed Abstract: The SH3 domain is a protein-protein interaction module commonly found in intracellular signaling and adaptor proteins. The SH3 domains of multiple endocytic proteins have been recently implicated in binding ubiquitin, which serves as a signal for diverse cellular processes including gene regulation, endosomal sorting, and protein destruction. Here we describe the solution NMR structure of ubiquitin in complex with an SH3 domain belonging to the yeast endocytic protein Sla1. The ubiquitin binding surface of the Sla1 SH3 domain overlaps substantially with the canonical binding surface for proline-rich ligands. Like many other ubiquitin-binding motifs, the SH3 domain engages the Ile44 hydrophobic patch of ubiquitin. A phenylalanine residue located at the heart of the ubiquitin-binding surface of the SH3 domain serves as a key specificity determinant. The structure of the SH3-ubiquitin complex explains how a subset of SH3 domains has acquired this non-traditional function.

PubMed: 17765920
DOI: 10.1016/j.jmb.2007.07.074

実験手法

SOLUTION NMR