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The formation of a covalent complex between a dipeptide ligand and the src SH2 domain
K J Alligood1, P S Charifson, R Crosby
1Glaxo Wellcome, Inc., Research Triangle Park, North Carolina 27709, USA.
Bioorganic & Medicinal Chemistry Letters
|January 1, 1999
Abstract:
The X-ray crystal structure of the src SH2 domain revealed the presence of a thiol residue (Cys 188) located proximal to the phosphotyrosine portion of a dipeptide ligand. An aldehyde bearing ligand (1) was designed to position an electrophilic carbonyl group in the vicinity of the thiol. X-ray crystallographic and NMR examination of the complex formed between (1) and the src SH2 domain revealed a hemithioacetal formed by addition of the thiol to the aldehyde group with an additional stabilizing hydrogen bond between the acetal hydroxyl and a backbone carbonyl.