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Automated multiple analysis of protein structures: Application to homology modeling of cytochromes P450
Author(s) -
Jean Pascale,
Pothier Joël,
Dansette Patrick M.,
Mansuy Daniel,
Viari Alain
Publication year - 1997
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/(sici)1097-0134(199707)28:3<388::aid-prot9>3.0.co;2-8
Subject(s) - homology modeling , computational biology , homology (biology) , computer science , protein structure , sequence homology , protein structure prediction , sequence alignment , loop modeling , structural alignment , structural bioinformatics , threading (protein sequence) , protein design , peptide sequence , biology , biochemistry , amino acid , gene , enzyme
A computational strategy for homology modeling, using several protein structures comparison, is described. This strategy implies a formalized definition of structural blocks common to several protein structures, a new program to compare these structures simultaneously, and the use of consensus matrices to improve sequence alignment between the structurally known and target proteins. Applying this method to cytochromes P450 led to the definition of 15 substructures common to P450 cam , P450 BM3 , and P450 terp , and to proposing a 3D model of P450 eryF . Proteins 28:388–404, 1997 © 1997 Wiley‐Liss, Inc.