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Identification of a key element for hydrogen‐bonding patterns between protein kinases and their inhibitors
Author(s) -
Katayama Naoko,
Orita Masaya,
Yamaguchi Tomohiko,
Hisamichi Hiroyuki,
Kuromitsu Sadao,
Kurihara Hiroyuki,
Sakashita Hitoshi,
Matsumoto Yuzo,
Fujita Shigeo,
Niimi Tatsuya
Publication year - 2008
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/prot.22207
Subject(s) - kinase , hydrogen bond , chemistry , linker , biochemistry , protein data bank , protein kinase a , tyrosine kinase , microbiology and biotechnology , signal transduction , biology , protein structure , computer science , molecule , organic chemistry , operating system
In this article, we report crystal structures for inhibitor‐kinase complexes in which the inhibitor has different binding orientations and hydrogen‐bonding patterns with extracellular‐signal regulated kinase 2 and insulin receptor tyrosine kinase. Our crystallographic studies, and sequence and structural analyses of 532 coordinates of kinases held in the Protein Data Bank, suggest that the length of the “specificity linker” described here is a key structural element of the hydrogen‐bonding patterns between protein kinases and their inhibitors. Proteins 2008. © 2008 Wiley‐Liss, Inc.