Synthesis of the l- and d-SH2 domain of the leukaemia oncogene Bcr-Abl.

ABSTRACT: The d- and l-versions of the Bcr-Abl SH2 domain (12.7 kDa) were synthesized. Key optimizations included pseudoproline incorporation, N-terminal hydrophilic tail addition and mild N-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.

SUBMITTER: Schmidt N 

PROVIDER: S-EPMC9347351 | biostudies-literature | 2022 Aug

REPOSITORIES: biostudies-literature