title: Divergence of interdomain geometry in two-domain proteins.
abstract: For homologous protein chains composed of two domains, we have determined the extent to which they conserve (1) their interdomain geometry and (2) the molecular structure of the domain interface. This work was carried out on 128 unique two-domain architectures. Of the 128, we find 75 conserve their interdomain geometry and the structure of their domain interface; 5 conserve their interdomain geometry but not the structure of their interface; and 48 have variable geometries and divergent interface structure. We describe how different types of interface changes or the absence of an interface is responsible for these differences in geometry. Variable interdomain geometries can be found in homologous structures with high sequence identities (70%).
authors.affiliation: MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, United Kingdom. jhh03@mrc-lmb.cam.ac.uk
authors.forename: Jung-Hoon
authors.initials: JH
authors.lastname: Han
authors.forename: Nicola
authors.initials: N
authors.lastname: Kerrison
authors.forename: Cyrus
authors.initials: C
authors.lastname: Chothia
authors.forename: Sarah A
authors.initials: SA
authors.lastname: Teichmann
mesh_terms: D019295:Computational Biology; D017434:Protein Structure, Tertiary; D011506:Proteins / Q000737:chemistry*; D017386:Sequence Homology, Amino Acid; D040681:Structural Homology, Protein
chemical_list: D011506:Proteins