ADAR Proteins: Structure and Catalytic Mechanism

被引：52

作者：

Goodman, Rena A. ^{[1
]}

Macbeth, Mark R. ^{[2
]}

Beal, Peter A. ^{[1
]}

机构：

[1] Univ Calif Davis, Dept Chem, Davis, CA 95616 USA

[2] Carnegie Mellon Univ, Dept Biol Sci, Pittsburgh, PA 15213 USA

来源：

ADENOSINE DEAMINASES ACTING ON RNA (ADARS) AND A-TO-I EDITING | 2012年 / 353卷

关键词：

DOUBLE-STRANDED-RNA; TRANSITION-STATE ANALOG; EDITING ADENOSINE-DEAMINASE; CRYSTAL-STRUCTURE; CYTIDINE DEAMINASE; INOSITOL HEXAKISPHOSPHATE; ESCHERICHIA-COLI; ACTIVE-SITE; UNWINDING ACTIVITY; BACILLUS-SUBTILIS;

D O I：

10.1007/82_2011_144

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

Since the discovery of the adenosine deaminase (ADA) acting on RNA (ADAR) family of proteins in 1988 (Bass and Weintraub, Cell 55:1089-1098, 1988) (Wagner et al. Proc Natl Acad Sci U S A 86:2647-2651, 1989), we have learned much about their structure and catalytic mechanism. However, much about these enzymes is still unknown, particularly regarding the selective recognition and processing of specific adenosines within substrate RNAs. While a crystal structure of the catalytic domain of human ADAR2 has been solved, we still lack structural data for an ADAR catalytic domain bound to RNA, and we lack any structural data for other ADARs. However, by analyzing the structural data that is available along with similarities to other deaminases, mutagenesis and other biochemical experiments, we have been able to advance the understanding of how these fascinating enzymes function.

引用

页码：1 / 33

页数：33

共 108 条

[61] An overview of cytidine deaminases [J].