Exploring the Leucine-Proline Binding Pocket of the Src SH3 Domain Using Structure-Based, Split-Pool Synthesis and Affinity-Based Selection
- 1 January 1998
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 120 (1) , 30-36
- https://doi.org/10.1021/ja972729m
Abstract
No abstract availableKeywords
This publication has 19 references indexed in Scilit:
- Exploring the Specificity Pockets of Two Homologous SH3 Domains Using Structure-Based, Split-Pool Synthesis and Affinity-Based SelectionJournal of the American Chemical Society, 1998
- Crystal structure of the Src family tyrosine kinase HckNature, 1997
- Molecular basis for the binding of SH3 ligands with non-peptide elements identified by combinatorial synthesisChemistry & Biology, 1996
- Protein Structure-Based Combinatorial Chemistry: Discovery of Non-Peptide Binding Elements to Src SH3 DomainJournal of the American Chemical Society, 1996
- Crystal structure of the nickel–iron hydrogenase from Desulfovibrio gigasNature, 1995
- High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptidesNature Structural & Molecular Biology, 1994
- An enantioselective approach to 3.alpha.-hydroxy-15-rippertene. Construction of the tetracyclic ring systemJournal of the American Chemical Society, 1993
- Generation and use of synthetic peptide combinatorial libraries for basic research and drug discoveryNature, 1991
- General method for rapid synthesis of multicomponent peptide mixturesInternational Journal of Peptide and Protein Research, 1991
- Cyanohydridoborate anion as a selective reducing agentJournal of the American Chemical Society, 1971