7DF9

Crystal of Arrestin2-V2Rpp-1-Fab30 complex

Summary for 7DF9

• Entry DOI: 10.2210/pdb7df9/pdb
• Descriptor: Beta-arrestin-1, VASOPRESSIN V2 RECEPTOR PHOSPHOPEPTIDE, FAB30 LIGHT CHAIN, ... (4 entities in total)
• Functional Keywords: arrestin, g-protein-coupled receptor, phosphopeptide, antibody fragment, signaling protein
• Biological source: Bos taurus (Bovine); More
• Total number of polymer chains: 4
• Total formula weight: 102849.80

Authors

Sun, J.P.,Yu, X.,Xiao, P.,He, Q.T.,Lin, J.Y.,Zhu, Z.L. (deposition date: 2020-11-06, release date: 2021-07-28, Last modification date: 2024-10-09)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.17 Å)