Crystal structure of arrestin-3 reveals the basis of the difference in receptor binding between two non-visual subtypes.
Crystal structure of arrestin-3 reveals the basis of the difference in receptor binding between two non-visual subtypes.
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DOI：
10.1016/j.jmb.2010.12.034
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发表时间：
2011-02-25
影响因子：
5.6
通讯作者：
Spiller BW
中科院分区：
文献类型：
--
作者：
Zhan X;Gimenez LE;Gurevich VV;Spiller BW
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. Here we report the first crystal structure of arrestin-3, solved at 3.0Å. Arrestin-3 is an elongated two-domain molecule with the overall fold and key inter-domain interactions that hold free protein in the basal conformation similar to the other subtypes. Arrestin-3 is the least selective member of the family, binding 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, consistent with increased flexibility. By swapping the corresponding elements between arrestin-2 and -3 we show that the presence of this loose structure correlates with reduced arrestin selectivity for activated receptor, consistent with a conformational change in this β-sheet upon receptor binding.
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