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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

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

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]

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