Dissecting protein–protein recognition sites

TLDR

Recognition sites in 70 protein–protein complexes were dissected into surface patches by clustering interface atoms. A simple geometric model reproduces the number and distribution of atoms within each patch. Small interfaces (<2000 Ų) typically form a single patch, whereas larger interfaces are multipatch; each patch has a buried core and solvent‑accessible rim, with the core’s distinctive amino‑acid composition aiding site identification. © 2002 Wiley‑Liss, Inc.; Proteins 47:334–343.

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 &lt;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.