期刊
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
卷 47, 期 3, 页码 334-343出版社
WILEY
DOI: 10.1002/prot.10085
关键词
molecular recognition; protein-protein interaction; interfaces; protein surface; residue clusters; amino acid composition
The recognition sites in 70 pair-wise protein-protein complexes of known three-dimensional structure are dissected in a set of surface patches by clustering atoms at the interface. When the interface buries <2000 Angstrom(2) of protein surface, the recognition sites usually form a single patch on the surface of each component protein. In contrast, larger interfaces are generally multipatch, with at least one pair of patches that are equivalent in size to a single-patch interface. Each recognition site, or patch within a site, contains a core made of buried interface atoms, surrounded by a rim of atoms that remain accessible to solvent in the complex. A simple geometric model reproduces the number and distribution of atoms within a patch. The rim is similar in composition to the rest of the protein surface, but the core has a distinctive amino acid composition, which may help in identifying potential protein recognition sites on single proteins of known structures. (C) 2002 Wiley-Liss, Inc.
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