rasH mutants deficient in GTP binding.
AUTOR(ES)
Der, C J
RESUMO
Single amino acid substitutions were introduced into a region of the rasH protein (residues 116, 117, and 119) homologous to a variety of diverse GTP-binding proteins. Each of the mutant p21 proteins displayed a significant reduction (10- to 5,000-fold) in GTP binding affinity. Activated rasH proteins deficient in GTP binding were unaltered in their ability to morphologically transform NIH 3T3 cells.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=367069Documentos Relacionados
- Dominant inhibitory mutations in the Mg(2+)-binding site of RasH prevent its activation by GTP.
- Isolation of ras GTP-binding mutants using an in situ colony-binding assay.
- Nucleotide sequence of the two rat cellular rasH genes.
- Antibodies specific for amino acid 12 of the ras oncogene product inhibit GTP binding.
- Identification and characterization of Myxococcus xanthus mutants deficient in calcofluor white binding.