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Strategies for the NMR‐Based Identification and Optimization of Allosteric Protein Kinase Inhibitors
Author(s) -
Jahnke Wolfgang,
Blommers Marcel J. J.,
Fernández César,
Zwingelstein Christian,
Amstutz René
Publication year - 2005
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200500100
Subject(s) - allosteric regulation , kinase , identification (biology) , computational biology , chemistry , small molecule , binding site , biochemistry , enzyme , biology , ecology
Caught coming in the back door . Kinases are important drug targets, and new methods for the identification of novel classes of kinase inhibitors are urgently needed. By using a spin‐labeled analogue of adenine (shown as a red star), second‐site NMR screening can identify allosteric kinase inhibitors (right) that bind outside of the ATP‐binding pocket and might have an interesting selectivity profile.