Please use this identifier to cite or link to this item: https://doi.org/10.1002/biot.201100139
DC FieldValue
dc.titleAn in silico approach for the discovery of CDK5/p25 interaction inhibitors
dc.contributor.authorZhang, B.
dc.contributor.authorCorbel, C.
dc.contributor.authorGuéritte, F.
dc.contributor.authorCouturier, C.
dc.contributor.authorBach, S.
dc.contributor.authorTan, V.B.C.
dc.date.accessioned2014-10-27T08:21:38Z
dc.date.available2014-10-27T08:21:38Z
dc.date.issued2011-07
dc.identifier.citationZhang, B., Corbel, C., Guéritte, F., Couturier, C., Bach, S., Tan, V.B.C. (2011-07). An in silico approach for the discovery of CDK5/p25 interaction inhibitors. Biotechnology Journal 6 (7) : 871-881. ScholarBank@NUS Repository. https://doi.org/10.1002/biot.201100139
dc.identifier.issn18606768
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/100068
dc.description.abstractThe lack of selectivity of all existing ATP competitive inhibitors for a single cyclin-dependent kinase (CDK) has led us to redirect the structure-based molecule design from targeting the classic ATP-binding pocket in CDK5 toward the CDK5/p25 interface. The aim was to seek novel inhibition mechanisms to interrupt protein-protein interactions. A combined strategy of alanine-scanning calculations for locating binding sites, virtual screening for small molecules, molecular dynamics simulations for examining the binding stability of virtual screening hits and bio-assays for testing the level of inhibition was set up and used to explore novel inhibitors capable of interrupting the interactions between the proteins, and consequently of inhibiting the kinase activity. Two compounds were shown to inhibit the complex formation between CDK5 and p25 through p25 binding. They could open avenues for the discovery of new types of structures that prevent interactions between CDK5 and p25 or other CDK and activator proteins, and, more importantly, provide leads in the development of selective inhibitors among CDKs. Accompanying article Corbel et al. © 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1002/biot.201100139
dc.sourceScopus
dc.subjectCDK5
dc.subjectMolecular dynamics
dc.subjectProtein-protein interaction inhibitor
dc.subjectVirtual screening
dc.subjectVirtural alanine scanning
dc.typeArticle
dc.contributor.departmentBIOLOGICAL SCIENCES
dc.description.doi10.1002/biot.201100139
dc.description.sourcetitleBiotechnology Journal
dc.description.volume6
dc.description.issue7
dc.description.page871-881
dc.identifier.isiut000292738100011
Appears in Collections:Staff Publications

Show simple item record
Files in This Item:
There are no files associated with this item.

SCOPUSTM   
Citations

15
checked on May 18, 2022

WEB OF SCIENCETM
Citations

14
checked on May 18, 2022

Page view(s)

128
checked on May 12, 2022

Google ScholarTM

Check

Altmetric


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.