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Titolo:
COMPARATIVE MODELING OF HUMAN RENIN - A RETROSPECTIVE EVALUATION OF THE MODEL WITH RESPECT TO THE X-RAY CRYSTAL-STRUCTURE
Autore:
FRAZAO C; TOPHAM C; DHANARAJ V; BLUNDELL TL;
Indirizzi:
UNIV LONDON BIRKBECK COLL,MOLEC BIOL LAB LONDON WC1E 7HX ENGLAND UNIV LONDON BIRKBECK COLL,DEPT CRYSTALLOG,ICRF,STRUCT MOLEC BIOL UNITLONDON WC1E 7HX ENGLAND
Titolo Testata:
Pure and applied chemistry
fascicolo: 1, volume: 66, anno: 1994,
pagine: 43 - 50
SICI:
0033-4545(1994)66:1<43:CMOHR->2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
ACID SUBSTITUTION TABLES; 3-DIMENSIONAL STRUCTURE; ASPARTIC PROTEINASES; PORCINE PEPSIN; SEQUENCE-ANALYSIS; RESOLUTION; SPECIFICITY; INHIBITOR; PREDICTION; DESIGN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
40
Recensione:
Indirizzi per estratti:
Citazione:
C. Frazao et al., "COMPARATIVE MODELING OF HUMAN RENIN - A RETROSPECTIVE EVALUATION OF THE MODEL WITH RESPECT TO THE X-RAY CRYSTAL-STRUCTURE", Pure and applied chemistry, 66(1), 1994, pp. 43-50

Abstract

A three-dimensional model of human renin has been constructed using COMPOSER, a rule-based approach to comparative modelling. The model wasconstructed from the three-dimensional structures of two homologous aspartic proteinases, pepsin and chymosin, which have been defined by X-ray analysis. The variable regions were obtained from aspartic proteinase structures for most of the loops, but also from unrelated structures where appropriate conformers were not available within the family. Using a 3.5 angstrom cut-off for pairs of equivalent atoms, 280 C-alpha atom pairs of the model and the experimentally defined structure superpose with an rmsd of 0.84 angstrom. Larger deviations occur in someof the loop regions, especially around residues 290 where there is a proline-rich sequence with CIS-peptides. The analysis shows that comparative modelling can give a reasonably accurate estimate of homologousprotein structures especially in the active-site region and that these provide a useful basis for structure-based design in the absence of experimental data.

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Documento generato il 30/11/20 alle ore 16:43:23