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Titolo:
A molecular-field-based similarity study of non-nucleoside HIV-1 reverse transcriptase inhibitors. 2. The relationship between alignment solutions obtained from conformationally rigid and flexible matching
Autore:
Mestres, J; Rohrer, DC; Maggiora, GM;
Indirizzi:
Pharmacia & Upjohn Inc, Comp Aided Drug Discovery, Kalamazoo, MI 49001 USAPharmacia & Upjohn Inc Kalamazoo MI USA 49001 ry, Kalamazoo, MI 49001 USA
Titolo Testata:
JOURNAL OF COMPUTER-AIDED MOLECULAR DESIGN
fascicolo: 1, volume: 14, anno: 2000,
pagine: 39 - 51
SICI:
0920-654X(200001)14:1<39:AMSSON>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
DRUG DESIGN; ELECTROSTATIC POTENTIALS; FORCE-FIELD; SUPERPOSITION; DERIVATIVES; RECOGNITION; RESOLUTION; DATABASES; QUERIES; SHAPE;
Keywords:
flexible-conformations; molecular alignments; molecular-field similarity; non-nucleoside HIV-1 reverse transcriptase inhibitors;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
48
Recensione:
Indirizzi per estratti:
Indirizzo: Rohrer, DC Pharmacia & Upjohn Inc, Comp Aided Drug Discovery, Kalamazoo, MI 49001 USA Pharmacia & Upjohn Inc Kalamazoo MI USA 49001 oo, MI 49001 USA
Citazione:
J. Mestres et al., "A molecular-field-based similarity study of non-nucleoside HIV-1 reverse transcriptase inhibitors. 2. The relationship between alignment solutions obtained from conformationally rigid and flexible matching", J COMPUT A, 14(1), 2000, pp. 39-51

Abstract

An analysis of the relationship among alignment solutions obtained from field-based matching of a representative set of rigid conformers of three non-nucleoside HIV-1 reverse transcriptase inhibitors and solutions obtained from flexible matching of the same conformers is presented. In some cases, different alignment solutions obtained from rigid matching converge to the same solution when conformational rigidity is relaxed, indicating that a reduced set of conformers per molecule may be sufficient in many field-based similarity studies. Furthermore, the results also indicate the importance ofgoing beyond the pairwise similarity level to obtain consistent solutions in flexible-matching studies. In this respect, the best conformationally flexible multi-molecule alignment obtained is found to be in good agreement with the relative binding geometry and orientation found experimentally fromprotein-ligand crystal structures. The rms separation between corresponding atoms in computed and 'experimental' sets of three inhibitor structures is 0.94 Angstrom.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 28/03/20 alle ore 13:14:21