NDLI: Crystal structure of the kinase domain of serum and glucocorticoid-regulated kinase 1 in complex with AMP

Content Provider	PubMed Central
Author	Zhao, Baoguang Lehr, Ruth Smallwood, Angela M. Ho, Thau F. Maley, Kathleen Randall, Tanya Head, Martha S. Koretke, Kristin K. Schnackenberg, Christine G.
Abstract	Serum and glucocorticoid-regulated kinase 1 (SGK1) is a serine/threonine protein kinase of the AGC family which participates in the control of epithelial ion transport and is implicated in proliferation and apoptosis. We report here the 1.9 Å crystal structure of the catalytic domain of inactive human SGK1 in complex with AMP–PNP. SGK1 exists as a dimer formed by two intermolecular disulfide bonds between Cys258 in the activation loop and Cys193. Although most of the SGK1 structure closely resembles the common protein kinase fold, the structure around the active site is unique when compared to most protein kinases. The αC helix is not present in this inactive form of SGK1 crystal structure; instead, the segment corresponding to the C helix forms a β-strand that is stabilized by the N-terminal segment of the activation loop through a short antiparallel β-sheet. Since the differences from other kinases occur around the ATP binding site, this structure can provide valuable insight into the design of selective and highly potent ATP-competitive inhibitors of SGK1 kinase.
Related Links	http://dx.doi.org/10.1110/ps.073161707
Ending Page	2769
Page Count	9
Starting Page	2761
File Format	PDF
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science : A Publication of the Protein Society
Issue Number	12
Volume Number	16
Language	English
Publisher	Cold Spring Harbor Laboratory Press
Publisher Date	2007-12-01
Access Restriction	Open
Rights Holder	Cold Spring Harbor Laboratory Press
Subject Keyword	Biochemistry Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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