Inference of functional regions in proteins by quantification of evolutionary constraints
AUTOR(ES)
Simon, Alexander L.
FONTE
The National Academy of Sciences
RESUMO
Likelihood estimates of local rates of evolution within proteins reveal that selective constraints on structure and function are quantitatively stable over billions of years of divergence. The stability of constraints produces an intramolecular clock that gives each protein a characteristic pattern of evolutionary rates along its sequence. This pattern allows the identification of constrained regions and, because the rate of evolution is a quantitative measure of the strength of the constraint, of their functional importance. We show that results from such analyses, which require only sequence alignments, are consistent with experimental and mutational data. The methodology has significant predictive power and may be used to guide structure–function studies for any protein represented by a modest number of homologs in sequence databases.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=122447Documentos Relacionados
- Natural variation in human membrane transporter genes reveals evolutionary and functional constraints
- Domain mobility in proteins: functional and evolutionary implications
- Evolutionary constraints in conserved nongenic sequences of mammals
- Novel Internal Regions of Fluorescent Proteins Undergo Divergent Evolutionary Patterns
- Characterization of Evolutionary Rates and Constraints in Three Mammalian Genomes