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Structural basis for the activity of pp60c-src protein tyrosine kinase inhibitors

✍ Scribed by Ninad V. Prabhu; Subeeh A. Siddiqui; John S. McMurray; B. Montgomery Pettitt

Publisher
Wiley (John Wiley & Sons)
Year
2001
Tongue
English
Weight
444 KB
Volume
59
Category
Article
ISSN
0006-3525

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✦ Synopsis

Conformational searches on three closely related pp60 c-src protein tyrosine kinase inhibitors of varying potencies were performed to determine a structural basis for their activity. The first was a linear peptide (PDNEYAFFQf), the second its 10-membered cyclic analogue, and the third a cyclic analogue with a para carboxyphenylalanine in place of one the F residues. A common backbone conformation with an antiparallel ␤-sheet-like geometry capped by similar ␤-turns was found for all three peptides, which may be a binding conformation and gives a candidate pharmacophore for further testing. The interaction between some polar side chains and between some of the aromatic rings may be important for maintaining the correct conformation. The differences in potencies of these inhibitors may be attributed to certain thermodynamic and chemical reasons.

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