Back

Xenon Explores Apparent and Cryptic Binding Sites

Iida, S.

2025-05-07 biophysics
10.1101/2025.04.30.651394 bioRxiv
Show abstract

Molecular binding sites of a protein tell us how to target the protein from their structural information, which is required for structure-based drug design. However, regardless of their importance, some binding sites, called cryptic binding (CB) sites, are not always readily apparent in the absence of ligands. The identification of CB sites from protein structures remains challenging, and no standard method has been proposed for this purpose. In this study, inspired by the observation of X-ray protein structures with noble gases, particularly xenon, I evaluate a xenon-based CB site identification strategy from their apo states by directly comparing its performance against benzene as a baseline probe. I performed atomistic molecular dynamics simulations of apo proteins with known CB sites in the presence of xenons. The simulations have revealed that xenons are likely to occupy not only apparent binding sites but also CB sites, implying that they serve as a probe to explore binding sites. O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=111 SRC="FIGDIR/small/651394v2_ufig1.gif" ALT="Figure 1"> View larger version (20K): org.highwire.dtl.DTLVardef@92907forg.highwire.dtl.DTLVardef@4c8538org.highwire.dtl.DTLVardef@1be1faforg.highwire.dtl.DTLVardef@1122a70_HPS_FORMAT_FIGEXP M_FIG C_FIG

Matching journals

The top 2 journals account for 50% of the predicted probability mass.

50% of probability mass above

"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.