title: Evolutionary predictions of binding surfaces and interactions.
abstract: Rapid progress in structural biology and whole-genome sequencing technology means that, for many protein families, structural and evolutionary information are readily available. Recent developments demonstrate how this information can be integrated to identify canonical determinants of protein structure and function. Among these determinants, those residues that are on protein surfaces are especially likely to form binding sites and are the logical choice for further mutational analysis and drug targeting.
authors.affiliation: Department of Molecular and Human Genetics, 1 Baylor Plaza, Baylor College of Medicine, Houston, Texas 77030, USA. lichtarge@bcm.tmc.edu
authors.forename: Olivier
authors.initials: O
authors.lastname: Lichtarge
authors.forename: Mathew E
authors.initials: ME
authors.lastname: Sowa
mesh_terms: D001665:Binding Sites / Q000502:physiology*; D020134:Catalytic Domain / Q000502:physiology; D019143:Evolution, Molecular; D005544:Forecasting; D006801:Humans; D008024:Ligands; D005810:Multigene Family; D011485:Protein Binding; D017510:Protein Folding; D025941:Protein Interaction Mapping; D016415:Sequence Alignment
chemical_list: D008024:Ligands