Structure-activity relationships of methionyl-tRNA synthetase: graphics modelling and genetic engineering
- 31 March 1987
- journal article
- Published by Elsevier in Journal of Molecular Graphics
- Vol. 5 (1), 18-21
- https://doi.org/10.1016/0263-7855(87)80039-5
Abstract
No abstract availableKeywords
This publication has 25 references indexed in Scilit:
- Identification of peptide sequences at the tRNA binding site of Escherichia coli methionyl-tRNA synthetaseBiochemistry, 1986
- Methionyl-tRNA synthetase from Escherichia coli: primary structure at the binding site for the 3'-end of tRNAfMetBiochemistry, 1985
- A large increase in enzyme–substrate affinity by protein engineeringNature, 1984
- Structural homology in the amino-terminal domains of two aminoacyl-tRNA synthetasesJournal of Molecular Biology, 1983
- Redesigning enzyme structure by site-directed mutagenesis: tyrosyl tRNA synthetase and ATP bindingNature, 1982
- Tyrosyl-tRNA synthetase forms a mononucleotide-binding foldJournal of Molecular Biology, 1982
- Crystal structure of Escherichia coli methionyl-tRNA synthetase at 2.5 Å resolutionJournal of Molecular Biology, 1982
- Methionyl-tRNA synthetase shows the nucleotide binding fold observed in dehydrogenasesNature, 1981
- Aminoacyl-tRNA Synthetases: General Features and Recognition of Transfer RNAsAnnual Review of Biochemistry, 1979
- Three-dimensional structure of d-glyceraldehyde-3-phosphate dehydrogenaseJournal of Molecular Biology, 1974