Electrostatic recognition in substrate binding to serine proteases.

ABSTRACT: Serine proteases of the Chymotrypsin family are structurally very similar but have very different substrate preferences. This study investigates a set of 9 different proteases of this family comprising proteases that prefer substrates containing positively charged amino acids, negatively charged amino acids, and uncharged amino acids with varying degree of specificity. Here, we show that differences in electrostatic substrate preferences can be predicted reliably by electrostatic molecular interaction fields employing customized GRID probes. Thus, we are able to directly link protease structures to their electrostatic substrate preferences. Additionally, we present a new metric that measures similarities in substrate preferences focusing only on electrostatics. It efficiently compares thes

SUBMITTER: Waldner BJ 

PROVIDER: S-EPMC6175425 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature