title: Identification of a key element for hydrogen-bonding patterns between protein kinases and their inhibitors.
abstract: 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.
authors.affiliation: Drug Discovery Research, Astellas Pharma Inc., 21 Miyukigaoka, Tsukuba, Ibaraki 305-8585, Japan.
authors.forename: Naoko
authors.initials: N
authors.lastname: Katayama
authors.forename: Masaya
authors.initials: M
authors.lastname: Orita
authors.forename: Tomohiko
authors.initials: T
authors.lastname: Yamaguchi
authors.forename: Hiroyuki
authors.initials: H
authors.lastname: Hisamichi
authors.forename: Sadao
authors.initials: S
authors.lastname: Kuromitsu
authors.forename: Hiroyuki
authors.initials: H
authors.lastname: Kurihara
authors.forename: Hitoshi
authors.initials: H
authors.lastname: Sakashita
authors.forename: Yuzo
authors.initials: Y
authors.lastname: Matsumoto
authors.forename: Shigeo
authors.initials: S
authors.lastname: Fujita
authors.forename: Tatsuya
authors.initials: T
authors.lastname: Niimi