1DDV

CRYSTAL STRUCTURE OF THE HOMER EVH1 DOMAIN WITH BOUND MGLUR PEPTIDE

1DDV の概要

• エントリーDOI: 10.2210/pdb1ddv/pdb
• 関連するPDBエントリー: 1DDW
• 分子名称: GLGF-DOMAIN PROTEIN HOMER, METABOTROPIC GLUTAMATE RECEPTOR MGLUR5 (3 entities in total)
• 機能のキーワード: protein-ligand complex, polyproline recognition, beta turn, signaling protein
• 由来する生物種: Rattus norvegicus (Norway rat); 詳細
• 細胞内の位置: Cytoplasm : Q9Z214; Cell membrane ; Multi-pass membrane protein : P31424
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 13332.94

構造登録者

Beneken, J.,Tu, J.C.,Xiao, B.,Worley, P.F.,Leahy, D.J. (登録日: 1999-11-11, 公開日: 2000-05-10, 最終更新日: 2024-02-07)

主引用文献

Beneken, J.,Tu, J.C.,Xiao, B.,Nuriya, M.,Yuan, J.P.,Worley, P.F.,Leahy, D.J.
Structure of the Homer EVH1 domain-peptide complex reveals a new twist in polyproline recognition.
Neuron, 26:143-154, 2000

PubMed Abstract: Homer EVH1 (Ena/VASP Homology 1) domains interact with proline-rich motifs in the cytoplasmic regions of group 1 metabotropic glutamate receptors (mGluRs), inositol-1,4,5-trisphosphate receptors (IP3Rs), and Shank proteins. We have determined the crystal structure of the Homer EVH1 domain complexed with a peptide from mGluR (TPPSPF). In contrast to other EVH1 domains, the bound mGluR ligand assumes an unusual conformation in which the side chains of the Ser-Pro tandem are oriented away from the Homer surface, and the Phe forms a unique contact. This unusual binding mode rationalizes conserved features of both Homer and Homer ligands that are not shared by other EVH1 domains. Site-directed mutagenesis confirms the importance of specific Homer residues for ligand binding. These results establish a molecular basis for understanding the biological properties of Homer-ligand complexes.

PubMed: 10798399
DOI: 10.1016/S0896-6273(00)81145-9

実験手法

X-RAY DIFFRACTION (1.9 Å)