| Literature DB >> 23153798 |
Samit K Bhattacharya1, Gary E Aspnes, Scott W Bagley, Markus Boehm, Arthur D Brosius, Leonard Buckbinder, Jeanne S Chang, Joseph Dibrino, Heather Eng, Kosea S Frederick, David A Griffith, Matthew C Griffor, Cristiano R W Guimarães, Angel Guzman-Perez, Seungil Han, Amit S Kalgutkar, Jacquelyn Klug-McLeod, Carmen Garcia-Irizarry, Jianke Li, Blaise Lippa, David A Price, James A Southers, Daniel P Walker, Liuqing Wei, Jun Xiao, Michael P Zawistoski, Xumiao Zhao.
Abstract
Previous drug discovery efforts identified classical PYK2 kinase inhibitors such as 2 and 3 that possess selectivity for PYK2 over its intra-family isoform FAK. Efforts to identify more kinome-selective chemical matter that stabilize a DFG-out conformation of the enzyme are described herein. Two sub-series of PYK2 inhibitors, an indole carboxamide-urea and a pyrazole-urea have been identified and found to have different binding interactions with the hinge region of PYK2. These leads proved to be more selective than the original classical inhibitors.Entities:
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Year: 2012 PMID： 23153798 DOI： 10.1016/j.bmcl.2012.10.039
Source DB: PubMed Journal: Bioorg Med Chem Lett ISSN： 0960-894X Impact factor: 2.823