Simulations of a specific inhibitor of the dishevelled PDZ domain

Xin Chen; Yuefan Deng

doi:10.1007/s00894-008-0377-x

Simulations of a specific inhibitor of the dishevelled PDZ domain

Xin Chen, Yuefan Deng

Mathematics

Research output: Contribution to journal › Article › peer-review

Abstract

The dishevelled (Dvl) PDZ domain is believed to play an essential role in the canonical and noncanonical Wnt signaling pathways, which are involved in embryo development as well as in tumorigenesis. Also, it binds directly to frizzled (Fz) receptors. An organic molecule (NSC668036) from the National Cancer Institute small-molecule library has been identified to be able to bind to the Dvl PDZ domain. Molecular dynamics simulation was used to provide detailed analyses of the binding between them.

Original language	English (US)
Pages (from-to)	91-96
Number of pages	6
Journal	Journal of Molecular Modeling
Volume	15
Issue number	1
DOIs	https://doi.org/10.1007/s00894-008-0377-x
State	Published - 2009

Keywords

Dishevelled PDZ domain
Molecular dynamics
Protein docking

ASJC Scopus subject areas

Catalysis
Computer Science Applications
Physical and Theoretical Chemistry
Organic Chemistry
Inorganic Chemistry
Computational Theory and Mathematics

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10.1007/s00894-008-0377-x

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KW - Protein docking

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Simulations of a specific inhibitor of the dishevelled PDZ domain

Abstract

Keywords

ASJC Scopus subject areas

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