3NYN

Crystal Structure of G Protein-Coupled Receptor Kinase 6 in Complex with Sangivamycin

3NYN の概要

• エントリーDOI: 10.2210/pdb3nyn/pdb
• 関連するPDBエントリー: 2ACX 3NYO
• 分子名称: G protein-coupled receptor kinase 6, SANGIVAMYCIN, SULFATE ION, ... (5 entities in total)
• 機能のキーワード: kinase, grk, rgs homology domain, g protein-coupled receptor kinase, transferase
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Membrane; Lipid-anchor: P43250
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 134107.24

構造登録者

Tesmer, J.J.G.,Singh, P. (登録日: 2010-07-15, 公開日: 2010-09-22, 最終更新日: 2024-02-21)

主引用文献

Boguth, C.A.,Singh, P.,Huang, C.C.,Tesmer, J.J.
Molecular basis for activation of G protein-coupled receptor kinases.
Embo J., 29:3249-3259, 2010

PubMed Abstract: G protein-coupled receptor (GPCR) kinases (GRKs) selectively recognize and are allosterically regulated by activated GPCRs, but the molecular basis for this interaction is not understood. Herein, we report crystal structures of GRK6 in which regions known to be critical for receptor phosphorylation have coalesced to stabilize the kinase domain in a closed state and to form a likely receptor docking site. The crux of this docking site is an extended N-terminal helix that bridges the large and small lobes of the kinase domain and lies adjacent to a basic surface of the protein proposed to bind anionic phospholipids. Mutation of exposed, hydrophobic residues in the N-terminal helix selectively inhibits receptor, but not peptide phosphorylation, suggesting that these residues interact directly with GPCRs. Our structural and biochemical results thus provide an explanation for how receptor recognition, phospholipid binding, and kinase activation are intimately coupled in GRKs.

PubMed: 20729810
DOI: 10.1038/emboj.2010.206

実験手法

X-RAY DIFFRACTION (2.72 Å)