Anchor Residues Govern Binding and Folding of an Intrinsically Disordered Domain.
Sign Up to like & getrecommendations! Published in 2022 at "ACS chemical biology"
DOI: 10.1021/acschembio.2c00619
Abstract: Minimal protein mimics have yielded novel classes of protein-protein interaction inhibitors; however, this success has not been extended to targeting intrinsically disordered proteins, which represent a significant proportion of important therapeutic targets. We sought to… read more here.
Keywords: binding folding; intrinsically disordered; govern binding; anchor residues ... See more keywords
Reshaping acetylated peptide selectivity between human BET Brd2 bromodomains BD-I and BD-II in glioblastoma by rationally grafting secondary anchor residues.
Sign Up to like & getrecommendations! Published in 2018 at "General physiology and biophysics"
DOI: 10.4149/gpb_2017063
Abstract: Selective inhibition of BET Brd2 BD-I and BD-II bromodomains is expected to elicit subtle pharmacological difference in anti-glioblastoma therapy. Here, structural basis and energetic property underlying the selective interaction of acetylated peptide ligands with Brd2… read more here.
Keywords: secondary anchor; anchor residues; acetylated peptide; peptide selectivity ... See more keywords