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

被引：42

作者：

Min, Kyungjin ^{[1
]}

Yoon, Hye-Jin ^{[1
]}

Park, Ji Young ^{[2
]}

Baidya, Mithu ^{[3
]}

Dwivedi-Agnihotri, Hemlata ^{[3
]}

Maharana, Jagannath ^{[3
]}

Chaturvedi, Madhu ^{[3
]}

Chung, Ka Young ^{[2
]}

Shukla, Arun K. ^{[3
]}

Lee, Hyung Ho ^{[1
]}

机构：

[1] Seoul Natl Univ, Coll Nat Sci, Dept Chem, Seoul 08826, South Korea

[2] Sungkyunkwan Univ, Sch Pharm, Suwon 16419, South Korea

[3] Indian Inst Technol, Biol Sci & Bioengn, Kanpur 208016, Uttar Pradesh, India

来源：

STRUCTURE | 2020年 / 28卷 / 09期

基金：

新加坡国家研究基金会; 英国惠康基金;

关键词：

RECEPTOR-BINDING; VISUAL ARRESTIN; PROTEIN; PHOSPHORYLATION; RECRUITMENT; ACTIVATION; MECHANISM; ANGSTROM; ROLES; MODEL;

D O I：

10.1016/j.str.2020.06.002

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：

beta-Arrestins (beta arrs) critically regulate G-protein-coupled receptor (GPCR) signaling and trafficking. beta arrs have two isoforms, beta arr1 and beta arr2. Receptor phosphorylation is a key determinant for the binding of beta arrs, and understanding the intricate details of receptor-beta arr interaction is the next frontier in GPCR structural biology. The high-resolution structure of active beta arr1 in complex with a phosphopeptide derived from GPCR has been revealed, but that of beta arr2 remains elusive. Here, we present a 2.3-A crystal structure of beta arr2 in complex with a phosphopeptide (C7pp) derived from the carboxyl terminus of CXCR7. The structural analysis of C7pp-bound beta arr2 reveals key differences from the previously determined active conformation of beta arr1. One of the key differences is that C7pp-bound beta arr2 shows a relatively small inter-domain rotation. Antibody-fragment-based conformational sensor and hydrogen/deuterium exchange experiments further corroborated the structural features of beta arr2 and suggested that beta arr2 adopts a range of inter-domain rotations.

引用

页码：1014 / +

页数：14

共 56 条

[11] X-ray crystal structure of arrestin from bovine rod outer segments [J].

Granzin, J ;

Wilden, U ;

Choe, HW ;

Labahn, J ;

Krafft, B ;

Büldt, G .

NATURE, 1998, 391 (6670) :918-921

[12] Structural evidence for the role of polar core residue Arg175 in arrestin activation [J].

Granzin, Joachim ;

Stadler, Andreas ;

Cousin, Anneliese ;

Schlesinger, Ramona ;

Batra-Safferling, Renu .

SCIENTIFIC REPORTS, 2015, 5

[13] Crystal Structure of p44, a Constitutively Active Splice Variant of Visual Arrestin [J].

Granzin, Joachim ;

Cousin, Anneliese ;

Weirauch, Moritz ;

Schlesinger, Ramona ;

Bueldt, Georg ;

Batra-Safferling, Renu .

JOURNAL OF MOLECULAR BIOLOGY, 2012, 416 (05) :611-618

[14] The molecular acrobatics of arrestin activation [J].

Gurevich, VV ;

Gurevich, EV .

TRENDS IN PHARMACOLOGICAL SCIENCES, 2004, 25 (02) :105-111

[15] Crystal structure of β-arrestin at 1.9 Å:: Possible mechanism of receptor binding and membrane translocation [J].

Han, M ;

Gurevich, VV ;

Vishnivetskiy, SA ;

Sigler, PB ;

Schubert, C .

STRUCTURE, 2001, 9 (09) :869-880

[16] The 2.8 Å crystal structure of visual arrestin:: A model for arrestin's regulation [J].

Hirsch, JA ;

Schubert, C ;

Gurevich, VV ;

Sigler, PB .

CELL, 1999, 97 (02) :257-269

[17] Rapid Uptake and Degradation of CXCL12 Depend on CXCR7 Carboxyl-terminal Serine/Threonine Residues [J].

Hoffmann, Frauke ;

Mueller, Wiebke ;

Schuetz, Dagmar ;

Penfold, Mark E. ;

Wong, Yung H. ;

Schulz, Stefan ;

Stumm, Ralf .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2012, 287 (34) :28362-28377

[18] XDS [J].

Kabsch, Wolfgang .

ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 2010, 66 :125-132

[19] Structure of an Arrestin2-Clathrin Complex Reveals a Novel Clathrin Binding Domain That Modulates Receptor Trafficking [J].

Kang, Dong Soo ;

Kern, Ronald C. ;

Puthenveedu, Manojkumar A. ;

von Zastrow, Mark ;

Williams, John C. ;

Benovic, Jeffrey L. .

JOURNAL OF BIOLOGICAL CHEMISTRY, 2009, 284 (43) :29860-29872

[20] Crystal structure of rhodopsin bound to arrestin by femtosecond X-ray laser [J].

Kang, Yanyong ;

Zhou, X. Edward ;

Gao, Xiang ;

He, Yuanzheng ;

Liu, Wei ;

Ishchenko, Andrii ;

Barty, Anton ;

Sathish, D. ;

Yefanov, Oleksandr ;

Han, Gye Won ;

Xu, Qingping ;

de Waal, Parker W. ;

Ke, Jiyuan ;

Tan, M. H. Eileen ;

Zhang, Chenghai ;

Moeller, Arne ;

West, Graham M. ;

Pascal, Bruce D. ;

Van Eps, Ned ;

Caro, Lydia N. ;

Vishnivetskiy, Sergey A. ;

Lee, Regina J. ;

Suino-Powell, Kelly M. ;

Gu, Xin ;

Pal, Kuntal ;

Ma, Jinming ;

Zhi, Xiaoyong ;

Boutet, Sebastien ;

Williams, Garth J. ;

Messerschmidt, Marc ;

Gati, Cornelius ;

Zatsepin, Nadia A. ;

Wang, Dingjie ;

James, Daniel ;

Basu, Shibom ;

Roy-Chowdhury, Shatabdi ;

Conrad, Chelsie E. ;

Coe, Jesse ;

Liu, Haiguang ;

Lisova, Stella ;

Kupitz, Christopher ;

Grotjohann, Ingo ;

Fromme, Raimund ;

Jiang, Yi ;

Tan, Minjia ;

Yang, Huaiyu ;

Li, Jun ;

Wang, Meitian ;

Zheng, Zhong ;

Li, Dianfan .

NATURE, 2015, 523 (7562) :561-+

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