7DFA

Crystal of Arrestin2-V2Rpp-4-Fab30 complex

7DFA の概要

• エントリーDOI: 10.2210/pdb7dfa/pdb
• 分子名称: Beta-arrestin-1, FAB30 HEAVY CHAIN, FAB30 LIGHT CHAIN, ... (5 entities in total)
• 機能のキーワード: arrestin, g-protein-coupled receptor, phosphopeptide, antibody fragment, signaling protein
• 由来する生物種: Bos taurus (Bovine); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 102763.69

構造登録者

Sun, J.P.,Yu, X.,Xiao, P.,He, Q.T.,Lin, J.Y.,Zhu, Z.L. (登録日: 2020-11-06, 公開日: 2021-07-28, 最終更新日: 2024-11-13)

主引用文献

He, Q.T.,Xiao, P.,Huang, S.M.,Jia, Y.L.,Zhu, Z.L.,Lin, J.Y.,Yang, F.,Tao, X.N.,Zhao, R.J.,Gao, F.Y.,Niu, X.G.,Xiao, K.H.,Wang, J.,Jin, C.,Sun, J.P.,Yu, X.
Structural studies of phosphorylation-dependent interactions between the V2R receptor and arrestin-2.
Nat Commun, 12:2396-2396, 2021

PubMed Abstract: Arrestins recognize different receptor phosphorylation patterns and convert this information to selective arrestin functions to expand the functional diversity of the G protein-coupled receptor (GPCR) superfamilies. However, the principles governing arrestin-phospho-receptor interactions, as well as the contribution of each single phospho-interaction to selective arrestin structural and functional states, are undefined. Here, we determined the crystal structures of arrestin2 in complex with four different phosphopeptides derived from the vasopressin receptor-2 (V2R) C-tail. A comparison of these four crystal structures with previously solved Arrestin2 structures demonstrated that a single phospho-interaction change results in measurable conformational changes at remote sites in the complex. This conformational bias introduced by specific phosphorylation patterns was further inspected by FRET and H NMR spectrum analysis facilitated via genetic code expansion. Moreover, an interdependent phospho-binding mechanism of phospho-receptor-arrestin interactions between different phospho-interaction sites was unexpectedly revealed. Taken together, our results provide evidence showing that phospho-interaction changes at different arrestin sites can elicit changes in affinity and structural states at remote sites, which correlate with selective arrestin functions.

PubMed: 33888704
DOI: 10.1038/s41467-021-22731-x

実験手法

X-RAY DIFFRACTION (2.54 Å)