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PMID: 10333745 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Review

Protein-RNA recognition.

Biopolymers ·Vol. 48 ·No. 2-3 ·1998-00-00 ·Pages 181-95

De Guzman RN, Turner RB, Summers MF

Abstract

The x-ray structure of the glutamine aminoacyl tRNA synthetase bound to its cognate tRNA(Gln) and ATP was reported by Steitz and co-workers in 1989, providing the first high resolution structure of a protein-RNA complex. Since then, high resolution structures have been reported for RNA complexes with five other tRNA synthetases, the elongation factor Tu, the bacteriophage MS2 coat protein, the human spliceosomal U1A and U2B"-U1A' proteins, and the HIV-1 nucleocapsid protein. Although the number of high resolution structures of protein-RNA complexes are rather small, some general themes have begun to emerge regarding the nature and mechanisms of protein-RNA recognition.

MeSH Terms
Amino Acyl-tRNA Synthetases/metabolism Humans Models, Molecular Nucleic Acid Conformation RNA-Binding Proteins/metabolism
Chemicals
RNA-Binding Proteins Amino Acyl-tRNA Synthetases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
De Guzman R N
Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, University of Maryland, Baltimore 21250, USA.
Turner R B
Summers M F
Article Info
Journal
Biopolymers
Abbr.
Biopolymers
ISSN
0006-3525
Published
1998-00-00
Pages
181-95
Language
English
Region
United States
NLM ID
0372525
Subset
IM
Grants
NIGMS NIH HHS · GM42561 · United States
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