title: Diversity in protein domain superfamilies.
abstract: Whilst ∼93% of domain superfamilies appear to be relatively structurally and functionally conserved based on the available data from the CATH-Gene3D domain classification resource, the remainder are much more diverse. In this review, we consider how domains in some of the most ubiquitous and promiscuous superfamilies have evolved, in particular the plasticity in their functional sites and surfaces which expands the repertoire of molecules they interact with and actions performed on them. To what extent can we identify a core function for these superfamilies which would allow us to develop a 'domain grammar of function' whereby a protein's biological role can be proposed from its constituent domains? Clearly the first step is to understand the extent to which these components vary and how changes in their molecular make-up modifies function.
authors.affiliation: Institute of Structural and Molecular Biology, UCL, 627 Darwin Building, Gower Street, WC1E 6BT, UK.
authors.forename: Sayoni
authors.initials: S
authors.lastname: Das
authors.affiliation: Institute of Structural and Molecular Biology, UCL, 627 Darwin Building, Gower Street, WC1E 6BT, UK.
authors.forename: Natalie L
authors.initials: NL
authors.lastname: Dawson
authors.affiliation: Institute of Structural and Molecular Biology, UCL, 627 Darwin Building, Gower Street, WC1E 6BT, UK. Electronic address: c.orengo@ucl.ac.uk.
authors.forename: Christine A
authors.initials: CA
authors.lastname: Orengo
mesh_terms: D000595:Amino Acid Sequence; D008958:Models, Molecular; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000145:classification* / Q000378:metabolism*
chemical_list: D011506:Proteins