title: Evolution of protein function, from a structural perspective.
abstract: The recent growth in structural data, and ensuing analyses, have revealed the structural and functional versatility of protein families. With respect to enzymes, local active-site mutations, variations in surface loops and recruitment of additional domains accommodate the diverse substrate specificities and catalytic activities observed within several superfamilies. Conversely, some functions have more than one structural solution, having evolved independently several times during evolution. Combined with the existence of multi-functional genes, which have arisen by gene recruitment, these phenomena must be considered in the process of genome annotation.
authors.affiliation: Biomolecular Structure and Modelling Unit Department of Biochemistry and Molecular Biology, University College London, Gower Street, London,WC1E 6BT, UK.
authors.forename: A E
authors.initials: AE
authors.lastname: Todd
authors.forename: C A
authors.initials: CA
authors.lastname: Orengo
authors.forename: J M
authors.initials: JM
authors.lastname: Thornton
mesh_terms: D000818:Animals; D002384:Catalysis; D004798:Enzymes / Q000235:genetics / Q000502:physiology*; D019143:Evolution, Molecular; D006801:Humans; D017510:Protein Folding; D013329:Structure-Activity Relationship; D013379:Substrate Specificity
chemical_list: D004798:Enzymes