Abstract

Abstract The recognition sites in 70 pairwise 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 Å 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. Proteins 2002;47:334–343. © 2002 Wiley‐Liss, Inc.

Keywords

Interface (matter)Surface (topology)CrystallographyAmino acidProtein structureCluster analysisPairwise comparisonMolecular recognitionChemistrySurface proteinBiological systemGeometryChemical physicsComputer scienceBiologyMoleculeMathematicsArtificial intelligenceBiochemistry

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Year
2002
Type
article
Volume
47
Issue
3
Pages
334-343
Citations
570
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Pinak Chakrabarti, Joël Janin (2002). Dissecting protein–protein recognition sites. Proteins Structure Function and Bioinformatics , 47 (3) , 334-343. https://doi.org/10.1002/prot.10085

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DOI
10.1002/prot.10085