1EH2

STRUCTURE OF THE SECOND EPS15 HOMOLOGY DOMAIN OF HUMAN EPS15, NMR, 20 STRUCTURES

1EH2 の概要

• エントリーDOI: 10.2210/pdb1eh2/pdb
• NMR情報: BMRB: 4184
• 分子名称: EPS15, CALCIUM ION (2 entities in total)
• 機能のキーワード: calcium binding, signaling domain, npf binding, ef-hand, eh domain
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm. Isoform 2: Early endosome membrane; Peripheral membrane protein; Cytoplasmic side: P42566
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 11975.89

構造登録者

De Beer, T.,Carter, R.E.,Lobel-Rice, K.E.,Sorkin, A.,Overduin, M. (登録日: 1998-07-10, 公開日: 1999-07-22, 最終更新日: 2024-05-22)

主引用文献

de Beer, T.,Carter, R.E.,Lobel-Rice, K.E.,Sorkin, A.,Overduin, M.
Structure and Asn-Pro-Phe binding pocket of the Eps15 homology domain.
Science, 281:1357-1360, 1998

PubMed Abstract: Eps15 homology (EH) domains are eukaryotic signaling modules that recognize proteins containing Asn-Pro-Phe (NPF) sequences. The structure of the central EH domain of Eps15 has been solved by heteronuclear magnetic resonance spectroscopy. The fold consists of a pair of EF hand motifs, the second of which binds tightly to calcium. The NPF peptide is bound in a hydrophobic pocket between two alpha helices, and binding is mediated by a critical aromatic interaction as revealed by structure-based mutagenesis. The fold is predicted to be highly conserved among 30 identified EH domains and provides a structural basis for defining EH-mediated events in protein trafficking and growth factor signaling.

PubMed: 9721102
DOI: 10.1126/science.281.5381.1357

実験手法

SOLUTION NMR