Crystal Structure of p44, a Constitutively Active Splice Variant of Visual Arrestin

被引：40

作者：

Granzin, Joachim ^{[1
]}

Cousin, Anneliese ^{[2
]}

Weirauch, Moritz ^{[2
]}

Schlesinger, Ramona ^{[2
,3
]}

Bueldt, Georg ^{[2
,4
]}

Batra-Safferling, Renu ^{[1
]}

机构：

[1] Forschungszentrum Julich, Inst Complex Syst, ICS Struct Biochem 6, D-52425 Julich, Germany

[2] Forschungszentrum Julich, Inst Complex Syst, ICS Mol Biophys 5, D-52425 Julich, Germany

[3] Free Univ Berlin, Inst Expt Phys, D-14195 Berlin, Germany

[4] Moscow Inst Phys & Technol, Res Educ Ctr Bionanophys, Dolgoprudnyi 141700, Russia

来源：

JOURNAL OF MOLECULAR BIOLOGY | 2012年 / 416卷 / 05期

关键词：

arrestin; splice variant; p44; rhodopsin; photoreceptor; ROD OUTER SEGMENTS; RHODOPSIN INTERACTIONS; RECEPTOR SPECIFICITY; MOLECULAR GRAPHICS; BOVINE RETINA; BINDING; LOCALIZATION; ACTIVATION; DYNAMICS; MODEL;

D O I：

10.1016/j.jmb.2012.01.028

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Visual arrestin specifically binds to photoactivated and phosphorylated rhodopsin and inactivates phototransduction. In contrast, the p44 splice variant can terminate phototransduction by binding to nonphosphorylated light-activated rhodopsin. Here we report the crystal structure of bovine p44 at a resolution of 1.85 angstrom. Compared to native arrestin, the p44 structure reveals significant differences in regions crucial for receptor binding, namely flexible loop V-VI and polar core regions. Additionally, electrostatic potential is remarkably positive on the N-domain and the C-domain. The p44 structure represents an active conformation that serves as a model to explain the 'constitutive activity' found in arrestin variants. (C) 2012 Elsevier Ltd. All rights reserved.

引用

页码：611 / 618

页数：8

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