6K3F

Crystal Structure of beta-Arrestin 2 in Complex with CXCR7 Phosphopeptide

Summary for 6K3F

• Entry DOI: 10.2210/pdb6k3f/pdb
• Descriptor: Beta-arrestin-2, Peptide from Atypical chemokine receptor 3 (3 entities in total)
• Functional Keywords: complex, signaling protein
• Biological source: Rattus norvegicus (Rat); More
• Total number of polymer chains: 12
• Total formula weight: 266302.35

Authors

Min, K.J.,Yoon, H.J.,Lee, H.H. (deposition date: 2019-05-18, release date: 2020-06-10, Last modification date: 2024-11-06)

Primary citation

Min, K.,Yoon, H.J.,Park, J.Y.,Baidya, M.,Dwivedi-Agnihotri, H.,Maharana, J.,Chaturvedi, M.,Chung, K.Y.,Shukla, A.K.,Lee, H.H.
Crystal Structure of beta-Arrestin 2 in Complex with CXCR7 Phosphopeptide.
Structure, 28:1014-1023.e4, 2020

PubMed Abstract: β-Arrestins (βarrs) critically regulate G-protein-coupled receptor (GPCR) signaling and trafficking. βarrs have two isoforms, βarr1 and βarr2. Receptor phosphorylation is a key determinant for the binding of βarrs, and understanding the intricate details of receptor-βarr interaction is the next frontier in GPCR structural biology. The high-resolution structure of active βarr1 in complex with a phosphopeptide derived from GPCR has been revealed, but that of βarr2 remains elusive. Here, we present a 2.3-Å crystal structure of βarr2 in complex with a phosphopeptide (C7pp) derived from the carboxyl terminus of CXCR7. The structural analysis of C7pp-bound βarr2 reveals key differences from the previously determined active conformation of βarr1. One of the key differences is that C7pp-bound βarr2 shows a relatively small inter-domain rotation. Antibody-fragment-based conformational sensor and hydrogen/deuterium exchange experiments further corroborated the structural features of βarr2 and suggested that βarr2 adopts a range of inter-domain rotations.

PubMed: 32579945
DOI: 10.1016/j.str.2020.06.002

Experimental method

X-RAY DIFFRACTION (2.3 Å)