1QJT

SOLUTION STRUCTURE OF THE APO EH1 DOMAIN OF MOUSE EPIDERMAL GROWTH FACTOR RECEPTOR SUBSTRATE 15, EPS15

1QJT の概要

• エントリーDOI: 10.2210/pdb1qjt/pdb
• NMR情報: BMRB: 4491
• 分子名称: EPIDERMAL GROWTH FACTOR RECEPTOR SUBSTRATE SUBSTRATE 15, EPS15 (1 entity in total)
• 機能のキーワード: growth factor, eh domain, eps15, ef-hand, solution structure, s100 protein
• 由来する生物種: MUS MUSCULUS (MOUSE)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 10672.21

構造登録者

Whitehead, B.,Tessari, M.,Carotenuto, A.,van Bergen en Henegouwen, P.M.,Vuister, G.W. (登録日: 1999-07-02, 公開日: 2000-01-23, 最終更新日: 2024-05-15)

主引用文献

Whitehead, B.,Tessari, M.,Carotenuto, A.,van Bergen en Henegouwen, P.M.,Vuister, G.W.
The Eh1 Domain of Eps15 is Structurally Classified as a Member of the S100 Subclass of EF-Hand Containing Proteins
Biochemistry, 38:11271-11277, 1999

PubMed Abstract: The Eps15 homology (EH) domain is a protein-protein interaction module that binds to proteins containing the asparagine-proline-phenylalanine (NPF) or tryptophan/phenylalanine-tryptophan (W/FW) motif. EH domain-containing proteins serve important roles in signaling and processes connected to transport, protein sorting, and organization of subcellular structure. Here, we report the solution structure of the apo form of the EH1 domain of mouse Eps15, as determined by high-resolution multidimensional heteronuclear NMR spectroscopy. The polypeptide folds into six alpha-helices and a short antiparallel beta-sheet. Additionally, it contains a long, structured, topologically unique C-terminal loop. Helices 2-5 form two EF-hand motifs. Structural similarity and Ca(2+) binding properties lead to classification of the EH1 domain as a member of the S100 subclass of EF-hand-containing proteins, albeit with a unique set of interhelical angles. Binding studies using an eight-residue NPF-containing peptide derived from RAB, the cellular cofactor of the HIV Rev protein, show a hydrophobic peptide-binding pocket formed by conserved tryptophan and leucine residues.

PubMed: 10471276
DOI: 10.1021/BI990922I

実験手法

SOLUTION NMR