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Biological and structural characterization of a Ras transforming mutation at the phenylalanine-156 residue, which is conserved in all members of the Ras superfamily

Authors :
Quilliam, Lawrence A.
Zhong, Sheng
Rabun, Kelly M.
Carpenter, John W.
South, Terri L.
Der, Channing J.
Campbell-Burk, Sharon
Source :
Proceedings of the National Academy of Sciences of the United States. Feb 28, 1995, Vol. 92 Issue 5, p1272, 5 p.
Publication Year :
1995

Abstract

NMR spectroscopic and assay studies of the structure and function of the carrier protein family of Ras proteins indicate the presence of a conserved phenylalanine-156 (F156) residue to be essential for maintaining the biological function and structure of Ras proteins. An F156 mutation in the wild-type Ras enhances the guanine nucleotide production, stimulated Ras transforming potential and affected the protein structure by disrupting the alpha-helix and beta-sheets.

Details

ISSN :
00278424
Volume :
92
Issue :
5
Database :
Gale General OneFile
Journal :
Proceedings of the National Academy of Sciences of the United States
Publication Type :
Academic Journal
Accession number :
edsgcl.16961107