Literature DB >> 17255140

Molecular basis for specificity in the druggable kinome: sequence-based analysis.

Jianping Chen1, Xi Zhang, Ariel Fernández.   

Abstract

MOTIVATION: Rational design of kinase inhibitors remains a challenge partly because there is no clear delineation of the molecular features that direct the pharmacological impact towards clinically relevant targets. Standard factors governing ligand affinity, such as potential for intermolecular hydrophobic interactions or for intermolecular hydrogen bonding do not provide good markers to assess cross reactivity. Thus, a core question in the informatics of drug design is what type of molecular similarity among targets promotes promiscuity and what type of molecular difference governs specificity. This work answers the question for a sizable screened sample of the human pharmacokinome including targets with unreported structure.
RESULTS: We show that drug design aimed at promoting pairwise interactions between ligand and kinase target actually fosters promiscuity because of the high conservation of the partner groups on or around the ATP-binding site of the kinase. Alternatively, we focus on a structural marker that may be reliably determined from sequence and measures dehydration propensities mostly localized on the loopy regions of kinases. Based on this marker, we construct a sequence-based kinase classifier that enables the accurate prediction of pharmacological differences. Our indicator is a microenvironmental descriptor that quantifies the propensity for water exclusion around preformed polar pairs. The results suggest that targeting polar dehydration patterns heralds a new generation of drugs that enable a tighter control of specificity than designs aimed at promoting ligand-kinase pairwise interactions. AVAILABILITY: The predictor of polar hot spots for dehydration propensity, or solvent-accessible hydrogen bonds in soluble proteins, named YAPView, may be freely downloaded from the University of Chicago website http://protlib.uchicago.edu/dloads.html. SUPPLEMENTARY INFORMATION: Supplementary data are available at Bioinformatics online.

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Year:  2007        PMID: 17255140      PMCID: PMC1950445          DOI: 10.1093/bioinformatics/btl666

Source DB:  PubMed          Journal:  Bioinformatics        ISSN: 1367-4803            Impact factor:   6.937


  25 in total

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3.  Protein-protein interactions: structurally conserved residues distinguish between binding sites and exposed protein surfaces.

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Journal:  Proc Natl Acad Sci U S A       Date:  2003-05-01       Impact factor: 11.205

4.  Dynamics of hydrogen bond desolvation in protein folding.

Authors:  Ariel Fernández; Tobin R Sosnick; Andrés Colubri
Journal:  J Mol Biol       Date:  2002-08-23       Impact factor: 5.469

5.  De novo prediction of three-dimensional structures for major protein families.

Authors:  Richard Bonneau; Charlie E M Strauss; Carol A Rohl; Dylan Chivian; Phillip Bradley; Lars Malmström; Tim Robertson; David Baker
Journal:  J Mol Biol       Date:  2002-09-06       Impact factor: 5.469

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8.  Hydrophobic bonding and accessible surface area in proteins.

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Journal:  Nature       Date:  1974-03-22       Impact factor: 49.962

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10.  The specificities of protein kinase inhibitors: an update.

Authors:  Jenny Bain; Hilary McLauchlan; Matthew Elliott; Philip Cohen
Journal:  Biochem J       Date:  2003-04-01       Impact factor: 3.857

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  6 in total

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4.  Molecular dynamics simulations show that conformational selection governs the binding preferences of imatinib for several tyrosine kinases.

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5.  An anticancer C-Kit kinase inhibitor is reengineered to make it more active and less cardiotoxic.

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6.  Protein under-wrapping causes dosage sensitivity and decreases gene duplicability.

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  6 in total

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