4PXF

Crystal structure of the active G-protein-coupled receptor opsin in complex with the finger-loop peptide derived from the full-length arrestin-1

4PXF の概要

• エントリーDOI: 10.2210/pdb4pxf/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900006
• 分子名称: Rhodopsin, S-arrestin, alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (9 entities in total)
• 機能のキーワード: retinal protein, photoreceptor, g-protein coupled receptor, phosphoprotein, photoreceptor protein, sensory transduction, transducer, transmembrane, vision, signaling protein, visual arrestin, desensitisation of the visual transduction cascade, binding to acticated and phosphorylated rhodopsin, rhodopsin, opsin
• 由来する生物種: Bos taurus (Bovine); 詳細
• 細胞内の位置: Membrane; Multi-pass membrane protein: P02699
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 42650.43

構造登録者

Szczepek, M.,Scheerer, P. (登録日: 2014-03-23, 公開日: 2014-09-17, 最終更新日: 2024-10-09)

主引用文献

Szczepek, M.,Beyriere, F.,Hofmann, K.P.,Elgeti, M.,Kazmin, R.,Rose, A.,Bartl, F.J.,von Stetten, D.,Heck, M.,Sommer, M.E.,Hildebrand, P.W.,Scheerer, P.
Crystal structure of a common GPCR-binding interface for G protein and arrestin.
Nat Commun, 5:4801-4801, 2014

PubMed Abstract: G-protein-coupled receptors (GPCRs) transmit extracellular signals to activate intracellular heterotrimeric G proteins (Gαβγ) and arrestins. For G protein signalling, the Gα C-terminus (GαCT) binds to a cytoplasmic crevice of the receptor that opens upon activation. A consensus motif is shared among GαCT from the Gi/Gt family and the 'finger loop' region (ArrFL1-4) of all four arrestins. Here we present a 2.75 Å crystal structure of ArrFL-1, a peptide analogue of the finger loop of rod photoreceptor arrestin, in complex with the prototypical GPCR rhodopsin. Functional binding of ArrFL to the receptor was confirmed by ultraviolet-visible absorption spectroscopy, competitive binding assays and Fourier transform infrared spectroscopy. For both GαCT and ArrFL, binding to the receptor crevice induces a similar reverse turn structure, although significant structural differences are seen at the rim of the binding crevice. Our results reflect both the common receptor-binding interface and the divergent biological functions of G proteins and arrestins.

PubMed: 25205354
DOI: 10.1038/ncomms5801

実験手法

X-RAY DIFFRACTION (2.75 Å)