Ontology highlight
ABSTRACT:
SUBMITTER: Schmidt N
PROVIDER: S-EPMC9347351 | biostudies-literature | 2022 Aug
REPOSITORIES: biostudies-literature
Schmidt Nina N Abendroth Frank F Vázquez Olalla O Hantschel Oliver O
RSC chemical biology 20220706 8
The d- and l-versions of the Bcr-Abl SH2 domain (12.7 kDa) were synthesized. Key optimizations included pseudoproline incorporation, <i>N</i>-terminal hydrophilic tail addition and mild <i>N</i>-acetoxy succinimide acetylation. Their folding and activity are as for the recombinant protein. Our results will enable engineering of mirror-image monobody antagonists of the central oncoprotein Bcr-Abl. ...[more]