Abstract
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 USA 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.
| Original language | English (US) |
|---|---|
| Title of host publication | Current Topics in Microbiology and Immunology |
| Pages | 1-33 |
| Number of pages | 33 |
| Volume | 353 |
| Edition | 1 |
| DOIs | |
| State | Published - 2012 |
Publication series
| Name | Current Topics in Microbiology and Immunology |
|---|---|
| Number | 1 |
| Volume | 353 |
| ISSN (Print) | 0070217X |
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ASJC Scopus subject areas
- Immunology and Allergy
- Microbiology (medical)
- Immunology
- Microbiology
Cite this
ADAR proteins : Structure and catalytic mechanism. / Goodman, Rena A.; MacBeth, Mark R.; Beal, Peter A.
Current Topics in Microbiology and Immunology. Vol. 353 1. ed. 2012. p. 1-33 (Current Topics in Microbiology and Immunology; Vol. 353, No. 1).Research output: Chapter in Book/Report/Conference proceeding › Chapter
}
TY - CHAP
T1 - ADAR proteins
T2 - Structure and catalytic mechanism
AU - Goodman, Rena A.
AU - MacBeth, Mark R.
AU - Beal, Peter A.
PY - 2012
Y1 - 2012
N2 - 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 USA 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.
AB - 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 USA 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.
UR - http://www.scopus.com/inward/record.url?scp=81855226703&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=81855226703&partnerID=8YFLogxK
U2 - 10.1007/82_2011_144
DO - 10.1007/82_2011_144
M3 - Chapter
C2 - 21769729
AN - SCOPUS:81855226703
SN - 9783642228001
VL - 353
T3 - Current Topics in Microbiology and Immunology
SP - 1
EP - 33
BT - Current Topics in Microbiology and Immunology
ER -