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Comparative modeling methods: Application to the family of the mammalian serine proteases
Author(s) -
Greer Jonathan
Publication year - 1990
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/prot.340070404
Subject(s) - homology modeling , proteases , serine , serine protease , computational biology , construct (python library) , loop modeling , sequence (biology) , protein structure , reliability (semiconductor) , protein family , homology (biology) , protein structure prediction , computer science , protease , biology , biological system , genetics , biochemistry , amino acid , physics , enzyme , power (physics) , quantum mechanics , programming language , gene
Comparative modeling methods are described that can be used to construct a three‐dimensional model structure of a new protein from knowledge of its sequence and of the experimental structure and sequences of other members of its homology family. The methods are illustrated with the mammalian serine protease family, for which seven experimental structures have been reported in the literature, and the sequence for over 35 different protein members of the family are available. The strategy for modeling these proteins is presented, and criteria are developed for determining and assigning the reliability of the modeled structure. Criteria are described that are specially designed to help detect cases in which it is likely that the local structure diverges significantly from the usual conformation of the family.