Probing the role of loop 2 in Ras function with unnatural amino acids

Authors :: Hyun-Ho Chung
Benson, David R.
Cornish, Virginia W.
Schultz, Peter G.
Source :: Proceedings of the National Academy of Sciences of the United States. Nov 1, 1993, Vol. 90 Issue 21, p10145, 5 p.
Publication Year :: 1993
Abstract: A study of the key residues Pro-34, Thr-35 and Ile-36 revealed the structural features needed for GTPase-activating protein (GAP) interaction and GTPase activity. The study employed the entire range of unnatural amino acid mutanenesis. GAP activation of Ras was curbed by the elimination of a single methyl group from Ile, proving that high specificity exists in protein-protein interaction.

Subjects :: Ras genes -- Analysis
Amino acids -- Analysis
G proteins -- Analysis
Science and technology

ISSN :: 00278424
Volume :: 90
Issue :: 21
Database :: Gale General OneFile
Journal :: Proceedings of the National Academy of Sciences of the United States
Publication Type :: Academic Journal
Accession number :: edsgcl.14832783

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