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rasH mutants deficient in GTP binding.
Author(s) -
Channing J. Der,
BinTao Pan,
Geoffrey M. Cooper
Publication year - 1986
Publication title -
molecular and cellular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.14
H-Index - 327
eISSN - 1067-8824
pISSN - 0270-7306
DOI - 10.1128/mcb.6.9.3291
Subject(s) - gtp' , biology , mutant , gtp binding protein regulators , biochemistry , binding site , plasma protein binding , g protein , dna binding protein , microbiology and biotechnology , receptor , enzyme , gene , transcription factor
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.

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