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Protein–RNA recognition
Author(s) -
De Guzman Roberto N.,
Turner Ryan B.,
Summers Michael F.
Publication year - 1998
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/(sici)1097-0282(1998)48:2<181::aid-bip7>3.0.co;2-l
Subject(s) - rna , transfer rna , chemistry , ef tu , biochemistry , rna binding protein , gene
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. © 1999 John Wiley & Sons, Inc. Biopoly 48: 181–195, 1998