Structural Basis of Single-Stranded RNA Recognition

Ana C. Messias and Michael Sattler*
Structural and Computational Biology, European Molecular Biology Laboratory (EMBL), Meyerhofstrasse 1, 69117 Heidelberg, Germany
Acc. Chem. Res., 2004, 37 (5), pp 279–287
DOI: 10.1021/ar030034m
Publication Date (Web): March 26, 2004
Copyright © 2004 American Chemical Society

Ana C. Messias, born in 1970 in Portugal, has a degree in Biochemistry from the University of Lisbon and completed a Ph.D. in Biochemistry at the ITQB, New University of Lisbon. She has been a postdoctoral fellow at EMBL since 2000 (supported by a FCT/FSE fellowship). Her interests are structure determination of biomolecules and the study of the relationship between structure and biological function.

Michael Sattler, born in 1965 in Germany, received a degree in Chemistry from the University of Frankfurt, followed by a Ph.D. with Christian Griesinger. In 1995, he joined Stephen W. Fesik at Abbott Laboratories, Chicago, as a postdoctoral fellow. His research group was established in 1997 and is interested in structural studies of molecular recognition during RNA processing and signal transduction by NMR.

Abstract

RNA is an ancient and highly versatile molecule that plays fundamental roles in all living organisms. Its molecular functions range from being a mediator of genetic information to the regulation of essential cellular processes. These functions are often accomplished in close association with RNA binding proteins. Over the past few years, a considerable number of high-resolution three-dimensional structures of important protein−RNA complexes have been determined. Here, we wish to discuss recent examples and highlight principles and distinct features of single-stranded RNA recognition by conserved RNA binding domains.

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History

  • Published In Issue May 18, 2004
  • Received August 25, 2003

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