1F8H

STRUCTURE OF THE SECOND EPS15 HOMOLOGY DOMAIN OF HUMAN EPS15 IN COMPLEX WITH PTGSSSTNPFR

1F8H の概要

• エントリーDOI: 10.2210/pdb1f8h/pdb
• 関連するPDBエントリー: 1eh2
• 分子名称: EPIDERMAL GROWTH FACTOR RECEPTOR SUBSTRATE 15, PTGSSSTNPFR, CALCIUM ION (3 entities in total)
• 機能のキーワード: complex, eh domain, npf, calcium binding, signaling domain, ef-hand, endocytosis-exocytosis complex, endocytosis/exocytosis
• 由来する生物種: Homo sapiens (human); 詳細
• 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: 2
• 化学式量合計: 11753.55

構造登録者

De Beer, T.,Hoofnagle, A.N.,Enmon, J.L.,Bowers, R.C.,Yamabhai, M.,Kay, B.K.,Overduin, M. (登録日: 2000-06-30, 公開日: 2000-11-01, 最終更新日: 2024-05-22)

主引用文献

de Beer, T.,Hoofnagle, A.N.,Enmon, J.L.,Bowers, R.C.,Yamabhai, M.,Kay, B.K.,Overduin, M.
Molecular mechanism of NPF recognition by EH domains.
Nat.Struct.Biol., 7:1018-1022, 2000

PubMed Abstract: Eps15 homology (EH) domains are protein interaction modules that recognize Asn-Pro-Phe (NPF) motifs in their biological ligands to mediate critical events during endocytosis and signal transduction. To elucidate the structural basis of the EH-NPF interaction, the solution structures of two EH-NPF complexes were solved using NMR spectroscopy. The first complex contains a peptide representing the Hrb C-terminal NPFL motif; the second contains a peptide in which an Arg residue substitutes the C-terminal Leu. The NPF residues are almost completely embedded in a hydrophobic pocket on the EH domain surface and the backbone of NPFX adopts a conformation reminiscent of the Asx-Pro type I beta-turn motif. The residue directly following NPF is crucial for recognition and is required to complete the beta-turn. Five amino acids on the EH surface mediate specific recognition of this residue through hydrophobic and electrostatic contacts. The complexes explain the selectivity of the second EH domain of Eps15 for NPF over DPF motifs and reveal a critical aromatic interaction that provides a conserved anchor for the recognition of FW, WW, SWG and HTF ligands by other EH domains.

PubMed: 11062555
DOI: 10.1038/80924

実験手法

SOLUTION NMR