Yeast aspartyl-tRNA synthetase residues interacting with tRNAAsp identity bases connectively contribute to tRNAAsp binding in the ground and transition-state complex and discriminate against non-cognate tRNAs-Reference-Cited by-同舟云学术

Yeast aspartyl-tRNA synthetase residues interacting with tRNAAsp identity bases connectively contribute to tRNAAsp binding in the ground and transition-state complex and discriminate against non-cognate tRNAs

Published:1999-08 Issue:4 Volume:291 Page:761-773
ISSN:0022-2836
Container-title:Journal of Molecular Biology
language:en
Short-container-title:Journal of Molecular Biology

Author:

Eriani Gilbert,Gangloff Jean

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference43 articles.

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4. The use of double mutants to detect structural changes in the active site of tyrosyl-tRNA synthetase;Carter;Cell,1984

5. Yeast tRNAAsp recognition by its cognate class II aminoacyl-tRNA synthetase;Cavarelli;Nature,1993

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