Related ArticlesDruggability indices for protein targets derived from NMR-based screening data.
J Med Chem. 2005 Apr 7;48(7):2518-25
Authors: Hajduk PJ, Huth JR, Fesik SW
An analysis of heteronuclear-NMR-based screening data is used to derive relationships between the ability of small molecules to bind to a protein and various parameters that describe the protein binding site. It is found that a simple model including terms for polar and apolar surface area, surface complexity, and pocket dimensions accurately predicts the experimental screening hit rates with an R(2) of 0.72, an adjusted R(2) of 0.65, and a leave-one-out Q(2) of 0.56. Application of the model to predict the druggability of protein targets not used in the training set correctly classified 94% of the proteins for which high-affinity, noncovalent, druglike leads have been reported. In addition to understanding the pocket characteristics that contribute to high-affinity binding, the relationships that have been defined allow for quantitative comparative analyses of protein binding sites for use in target assessment and validation, virtual ligand screening, and structure-based drug design.
[NMR paper] NMR fragment screening: tackling protein-protein interaction targets.
NMR fragment screening: tackling protein-protein interaction targets.
Related Articles NMR fragment screening: tackling protein-protein interaction targets.
Curr Opin Drug Discov Devel. 2005 May;8(3):365-73
Authors: Schade M, Oschkinat H
High-throughput screening of libraries containing compounds of 'drug-like' molecular weight has frequently resulted in no or poor drug candidates, especially when screening against demanding drug targets such as protein-protein interactions. Fragment-based lead discovery and optimization has evolved as a...
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11-25-2010 08:21 PM
[NMR paper] Assessing precision and accuracy of protein structures derived from NMR data.
Assessing precision and accuracy of protein structures derived from NMR data.
Related Articles Assessing precision and accuracy of protein structures derived from NMR data.
Proteins. 2005 Jun 1;59(4):655-61
Authors: Snyder DA, Bhattacharya A, Huang YJ, Montelione GT
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[NMR paper] High-throughput screening of structural proteomics targets using NMR.
High-throughput screening of structural proteomics targets using NMR.
Related Articles High-throughput screening of structural proteomics targets using NMR.
FEBS Lett. 2003 Sep 25;552(2-3):207-13
Authors: Galvão-Botton LM, Katsuyama AM, Guzzo CR, Almeida FC, Farah CS, Valente AP
We applied a high-throughput strategy for the screening of targets for structural proteomics of Xanthomonas axonopodis pv citri. This strategy is based on the rapid (1)H-(15)N HSQC NMR analysis of bacterial lysates containing selectively (15)N-labelled heterologous...
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11-24-2010 09:16 PM
[NMR paper] Privileged molecules for protein binding identified from NMR-based screening.
Privileged molecules for protein binding identified from NMR-based screening.
Related Articles Privileged molecules for protein binding identified from NMR-based screening.
J Med Chem. 2000 Sep 7;43(18):3443-7
Authors: Hajduk PJ, Bures M, Praestgaard J, Fesik SW
A statistical analysis of NMR-derived binding data on 11 protein targets was performed to identify molecular motifs that are preferred for protein binding. The analysis indicates that compounds which contain a biphenyl substructure preferentially bind to a wide range of proteins and...
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11-19-2010 08:29 PM
CoNSEnsX: an ensemble view of protein structures and NMR-derived experimental data.
CoNSEnsX: an ensemble view of protein structures and NMR-derived experimental data.
Related Articles CoNSEnsX: an ensemble view of protein structures and NMR-derived experimental data.
BMC Struct Biol. 2010 Oct 29;10(1):39
Authors: Angyan AF, Szappanos B, Perczel A, Gaspari Z
ABSTRACT: BACKGROUND: In conjunction with the recognition of the functional role of internal dynamics of proteins at various timescales, there is an emerging use of dynamic structural ensembles instead of individual conformers. These ensembles are usually substantially...
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CoNSEnsX: an ensemble view of protein structures and NMR-derived experimental data -
CoNSEnsX: an ensemble view of protein structures and NMR-derived experimental data - 7thSpace Interactive (press release)
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CoNSEnsX: an ensemble view of protein structures and NMR-derived experimental data
7thSpace Interactive (press release)
These ensembles are usually substantially more diverse than conventional NMR ensembles and eliminate the expectation that a single conformer should fulfill ...
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10-29-2010 09:32 PM
[BMNRC community] NMR-based screening: a powerful tool in fragment-based drug discovery
NMR-based screening: a powerful tool in fragment-based drug discovery
http://www.rsc.org/delivery/_ArticleLinking/DisplayHTMLArticleforfree.cfm?JournalCode=AN&Year=2007&ManuscriptID=b709658p&Iss=7
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09-02-2010 04:59 AM
[NMR paper] Conformational analysis of protein structures derived from NMR data.
Conformational analysis of protein structures derived from NMR data.
Related Articles Conformational analysis of protein structures derived from NMR data.
Proteins. 1993 Nov;17(3):232-51
Authors: MacArthur MW, Thornton JM
A study is presented of the conformational characteristics of NMR-derived protein structures in the Protein Data Bank compared to X-ray structures. Both ensemble and energy-minimized average structures are analyzed. We have addressed the problem using the methods developed for crystal structures by examining the distribution...
Druggability indices for protein targets derived from NMR-based screening data.
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