3P2D

Crystal structure of arrestin-3 reveals the basis of the difference in receptor binding between two non-visual subtypes

Summary for 3P2D

• Entry DOI: 10.2210/pdb3p2d/pdb
• Descriptor: Beta-arrestin-2 (1 entity in total)
• Functional Keywords: arrestin, signal transduction, cytosol, signaling protein
• Biological source: Bos taurus (bovine)
• Cellular location: Cytoplasm: P32120-2
• Total number of polymer chains: 2
• Total formula weight: 88470.96

Authors

Spiller, B.W.,Gurevich, V.V.,Zhan, X.,Gimenez, L.E. (deposition date: 2010-10-01, release date: 2011-01-26, Last modification date: 2023-09-06)

Primary citation

Zhan, X.,Gimenez, L.E.,Gurevich, V.V.,Spiller, B.W.
Crystal Structure of Arrestin-3 Reveals the Basis of the Difference in Receptor Binding Between Two Non-visual Subtypes.
J.Mol.Biol., 406:467-478, 2011

PubMed Abstract: Arrestins are multi-functional proteins that regulate signaling and trafficking of the majority of G protein-coupled receptors (GPCRs), as well as sub-cellular localization and activity of many other signaling proteins. We report the first crystal structure of arrestin-3, solved at 3.0 Å resolution. Arrestin-3 is an elongated two-domain molecule with overall fold and key inter-domain interactions that hold the free protein in the basal conformation similar to the other subtypes. Arrestin-3 is the least selective member of the family, binding a wide variety of GPCRs with high affinity and demonstrating lower preference for active phosphorylated forms of the receptors. In contrast to the other three arrestins, part of the receptor-binding surface in the arrestin-3 C-domain does not form a contiguous β-sheet, which is consistent with increased flexibility. By swapping the corresponding elements between arrestin-2 and arrestin-3 we show that the presence of this loose structure is correlated with reduced arrestin selectivity for activated receptors, consistent with a conformational change in this β-sheet upon receptor binding.

PubMed: 21215759
DOI: 10.1016/j.jmb.2010.12.034

Experimental method

X-RAY DIFFRACTION (3 Å)