Identifying medically relevant xenon protein targets by in silico screening of the structural proteome.

ABSTRACT: In a previous study, in silico screening of the binding of almost all proteins in the Protein Data Bank to each of the five noble gases xenon, krypton, argon, neon, and helium was reported. This massive and rich data set requires analysis to identify the gas-protein interactions that have the best binding strengths, those where the binding of the noble gas occurs at a site that can modulate the function of the protein, and where this modulation might generate clinically relevant effects. Here, we report a preliminary analysis of this data set using a rational, heuristic score based on binding strength and location. We report a partial prioritized list of xenon protein targets and describe how these data can be analyzed, using arginase and carbonic anhydrase as examples. Our aim is to make

SUBMITTER: Winkler DA 

PROVIDER: S-EPMC9480358 | biostudies-literature | 2023 Jan-Mar

REPOSITORIES: biostudies-literature