3T8O

Rhodopsin kinase (GRK1) L166K mutant at 2.5A resolution

3T8O の概要

• エントリーDOI: 10.2210/pdb3t8o/pdb
• 関連するPDBエントリー: 3c4w 3c4x
• 分子名称: Rhodopsin kinase, ADENOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (6 entities in total)
• 機能のキーワード: kinase domain, rgs homology (rh) domain, g-protein receptor kinase (gpcr), transferase
• 由来する生物種: Bos taurus (bovine,cow,domestic cattle,domestic cow)
• 細胞内の位置: Membrane ; Lipid- anchor : P28327
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 62104.99

構造登録者

Tesmer, J.J.G.,Singh, P.,Nance, M.R. (登録日: 2011-08-01, 公開日: 2012-06-06, 最終更新日: 2024-02-28)

主引用文献

Tesmer, J.J.,Nance, M.R.,Singh, P.,Lee, H.
Structure of a monomeric variant of rhodopsin kinase at 2.5 A resolution.
Acta Crystallogr.,Sect.F, 68:622-625, 2012

PubMed Abstract: G protein-coupled receptor kinase 1 (GRK1 or rhodopsin kinase) phosphorylates activated rhodopsin and initiates a cascade of events that results in the termination of phototransduction by the receptor. Although GRK1 seems to be a monomer in solution, seven prior crystal structures of GRK1 revealed a similar domain-swapped dimer interface involving the C-terminus of the enzyme. The influence of this interface on the overall conformation of GRK1 is not known. To address this question, the crystalline dimer interface was disrupted with a L166K mutation and the structure of GRK1-L166K was determined in complex with Mg(2+) · ATP to 2.5 Å resolution. GRK1-L166K crystallized in a novel space group as a monomer and exhibited little overall conformational difference from prior structures of GRK1, although the C-terminal domain-swapped region had reorganized owing to loss of the dimer interface.

PubMed: 22684056
DOI: 10.1107/S1744309112017435

実験手法

X-RAY DIFFRACTION (2.5 Å)