| Literature DB >> 9827998 |
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.Mesh:
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Year: 1998 PMID: 9827998 PMCID: PMC2143876 DOI: 10.1002/pro.5560071109
Source DB: PubMed Journal: Protein Sci ISSN: 0961-8368 Impact factor: 6.725