5AWT

Crystal structure of the SGIP1 mu homology domain in complex with an Eps15 fragment containing two DPF motifs (YDPFGGDPFKG)

5AWT の概要

• エントリーDOI: 10.2210/pdb5awt/pdb
• 関連するPDBエントリー: 5AWR 5AWS 5AWU
• 分子名称: SH3-containing GRB2-like protein 3-interacting protein 1, Epidermal growth factor receptor substrate 15, ZINC ION, ... (4 entities in total)
• 機能のキーワード: endocytosis, protein-protein interaction
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 32436.89

構造登録者

Shimada, A.,Yamaguchi, A.,Kohda, D. (登録日: 2015-07-08, 公開日: 2016-07-06, 最終更新日: 2024-11-06)

主引用文献

Shimada, A.,Yamaguchi, A.,Kohda, D.
Structural basis for the recognition of two consecutive mutually interacting DPF motifs by the SGIP1 mu homology domain.
Sci Rep, 6:19565-19565, 2016

PubMed Abstract: FCHo1, FCHo2, and SGIP1 are key regulators of clathrin-mediated endocytosis. Their μ homology domains (μHDs) interact with the C-terminal region of an endocytic scaffold protein, Eps15, containing fifteen Asp-Pro-Phe (DPF) motifs. Here, we show that the high-affinity μHD-binding site in Eps15 is a region encompassing six consecutive DPF motifs, while the minimal μHD-binding unit is two consecutive DPF motifs. We present the crystal structures of the SGIP1 μHD in complex with peptides containing two DPF motifs. The peptides bind to a novel ligand-binding site of the μHD, which is distinct from those of other distantly related μHD-containing proteins. The two DPF motifs, which adopt three-dimensional structures stabilized by sequence-specific intramotif and intermotif interactions, are extensively recognized by the μHD and are both required for binding. Thus, consecutive and singly scattered DPF motifs play distinct roles in μHD binding.

PubMed: 26822536
DOI: 10.1038/srep19565

実験手法

X-RAY DIFFRACTION (2.702 Å)