| Literature DB >> 15372308 |
K Aktories1, C Wilde, M Vogelsgesang.
Abstract
C3-like exoenzymes comprise a family of seven bacterial ADP-ribosyltransferases, which selectively modify RhoA, B, and C at asparagine-41. Crystal structures of C3 exoenzymes are available, allowing novel insights into the structure-function relationships of these exoenzymes. Because ADP-ribosylation specifically inhibits the biological functions of the low-molecular mass GTPases, C3 exoenzymes are established pharmacological tools to study the cellular functions of Rho GTPases. Recent studies, however, indicate that the functional consequences of C3-induced ADP-ribosylation are more complex than previously suggested. In the present review the basic properties of C3 exoenzymes are briefly summarized and new findings are reviewed.Entities:
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Year: 2004 PMID: 15372308 DOI: 10.1007/s10254-004-0034-4
Source DB: PubMed Journal: Rev Physiol Biochem Pharmacol ISSN: 0303-4240 Impact factor: 5.545