Abstract
We describe truncation and SAR studies to identify a pentapeptide that binds Cbl tyrosine kinase binding domain with a higher affinity than the parental peptide. The pentapeptide has an alternative binding mode that allows occupancy of a previously uncharacterized groove. A peptide library was used to map the binding site and define the interface landscape. Our results suggest that the pentapeptide is an ideal starting point for the development of inhibitors against Cbl driven diseases.
Original language | English (US) |
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Pages (from-to) | 3583-3587 |
Number of pages | 5 |
Journal | Journal of Medicinal Chemistry |
Volume | 55 |
Issue number | 7 |
DOIs | |
State | Published - Apr 12 2012 |
ASJC Scopus subject areas
- Molecular Medicine
- Drug Discovery