Article
Transition of arrestin into the active receptor-binding state requires an extended interdomain hinge.
The Journal of biological chemistry - 15 Nov 2002
Vishnivetskiy Sergey A, Hirsch Joel A, Velez Maria-Gabriela, Gurevich Yulia V, Gurevich Vsevolod V
Abstract excerpt
Arrestins selectively bind to the phosphorylated activated form of G protein-coupled receptors, thereby blocking further G protein activation. Structurally, arrestins consist of two domains topologically connected by a 12-residue long loop, which we term the "hinge" region. Both domains contain receptor-binding elements. The relative size and shape of arrestin and rhodopsin suggest that dramatic changes in...
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