Preservation of protein clefts in comparative models |
| |
Authors: | David Piedra Sergi Lois Xavier de la Cruz |
| |
Affiliation: | 1.Institut de Recerca Biomèdica,Barcelona,Spain;2.Institució Catalana de Recerca i Estudis Avan?ats (ICREA),Barcelona,Spain;3.Instituto de Biología Molecular de Barcelona, CID,Consejo Superior de Investigaciones Científicas (CSIC),Barcelona,Spain |
| |
Abstract: | Background Comparative, or homology, modelling of protein structures is the most widely used prediction method when the target protein has homologues of known structure. Given that the quality of a model may vary greatly, several studies have been devoted to identifying the factors that influence modelling results. These studies usually consider the protein as a whole, and only a few provide a separate discussion of the behaviour of biologically relevant features of the protein. Given the value of the latter for many applications, here we extended previous work by analysing the preservation of native protein clefts in homology models. We chose to examine clefts because of their role in protein function/structure, as they are usually the locus of protein-protein interactions, host the enzymes' active site, or, in the case of protein domains, can also be the locus of domain-domain interactions that lead to the structure of the whole protein. |
| |
Keywords: | |
本文献已被 SpringerLink 等数据库收录! |
|