title: Singular points of protein beta-sheets.
abstract: Protein beta-sheets can be regarded as surfaces. Two surfaces can be connected along a common edge to form a larger surface, or two edges of a surface can coalesce to form a closed sheet such as a beta-barrel. Singular points are locations where these connections are not perfect. In protein beta-sheets, a singular point is characterized by a residue separating two beta-ladders. In this paper, we study the singular points of protein beta-sheets from the surface topologic viewpoint, summarize our search results from the protein structural data in the Protein Data Bank, and present examples where singular points are near the active sites and may contribute to forming the proper relative positions of catalytic residues.
authors.affiliation: Department of Computer and Information Science, Indiana University Purdue University Indianapolis, 46202-5132, USA. wmliu@iupui.edu
authors.forename: W M
authors.initials: WM
authors.lastname: Liu
authors.forename: K C
authors.initials: KC
authors.lastname: Chou
mesh_terms: D001665:Binding Sites; D019731:Carbon-Nitrogen Ligases / Q000737:chemistry; D002384:Catalysis; D002480:Cellulase / Q000737:chemistry; D016208:Databases, Factual; D010088:Oxidoreductases / Q000737:chemistry; D017433:Protein Structure, Secondary; D012269:Ribosomal Proteins / Q000737:chemistry; D017385:Sequence Homology
chemical_list: D012269:Ribosomal Proteins; C049650:ribosomal protein L9; D010088:Oxidoreductases; C020094:duroquinol oxidase; D002480:Cellulase; D019731:Carbon-Nitrogen Ligases; C020828:GMP synthase (glutamine-hydrolyzing)