NDLI: Modulation of kinase-inhibitor interactions by auxiliary protein binding: crystallography studies on Aurora A interactions with VX-680 and with TPX2.

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Modulation of kinase-inhibitor interactions by auxiliary protein binding: crystallography studies on Aurora A interactions with VX-680 and with TPX2.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Yang, Jingsong Nurse, Kelvin Smallwood, Angela Calamari, Amy Koretke, Kristin Zhao, Baoguang Kirkpatrick, Robert B. Lai, Zhihong
Description	Country affiliation: United States Author Affiliation: Zhao B ( Department of Computational and Structural Chemistry, GlaxoSmithKline, 709 Swedeland Road, King of Prussia, PA 19406, USA. baoguang.zhao@gsk.com)
Abstract	VX-680, also known as MK-0457, is an ATP-competitive small molecule inhibitor of the Aurora kinases that has entered phase II clinical trials for the treatment of cancer. We have solved the cocrystal structure of AurA/TPX2/VX-680 at 2.3 A resolution. In the crystal structure, VX-680 binds to the active conformation of AurA. The glycine-rich loop in AurA adopts a unique bent conformation, forming a pi-pi interaction with the phenyl group of VX-680. In contrast, in the published AurA/VX-680 structure, VX-680 binds to AurA in the inactive conformation, interacting with a hydrophobic pocket only present in the inactive conformation. These data suggest that TPX2, a protein cofactor, can alter the binding mode of VX-680 with AurA. More generally, the presence of physiologically relevant cofactor proteins can alter the kinetics, binding interactions, and inhibition of enzymes, and studies with these multiprotein complexes may be beneficial to the discovery and optimization of enzyme inhibitors as therapeutic agents.
ISSN	09618368
e-ISSN	1469896X
DOI	10.1110/ps.036590.108
Journal	Protein Science
Issue Number	10
Volume Number	17
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2008-10-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Cell Cycle Proteins Chemistry Microtubule-associated Proteins Nuclear Proteins Piperazines Protein-serine-threonine Kinases Recombinant Proteins Aurora Kinases Catalytic Domain Metabolism Crystallography Crystallography, X-ray Protein Binding Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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