Synthesis of the <scp>l</scp>- and <scp>d</scp>-SH2 domain of the leukaemia oncogene Bcr-Abl-Reference-Cited by-同舟云学术

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

Published:2022 Issue:8 Volume:3 Page:1008-1012
ISSN:2633-0679
Container-title:RSC Chemical Biology
language:en
Short-container-title:RSC Chem. Biol.

Author:

Schmidt Nina¹^ORCID,Abendroth Frank²^ORCID,Vázquez Olalla²³^ORCID,Hantschel Oliver¹^ORCID

Affiliation:

1. Institute of Physiological Chemistry, University of Marburg, 35032, Marburg, Germany

2. Faculty of Chemistry, University of Marburg, 35032, Marburg, Germany

3. Center for Synthetic Microbiology (SYNMIKRO), University of Marburg, 35032, Marburg, Germany

Abstract

The d- and l-versions of the Bcr-Abl SH2 domain (12.7 kDa) were synthesized successfully and show similar folding as compared to a recombinantly expressed version.

Funder

Deutsche Forschungsgemeinschaft

H2020 European Research Council

Publisher

Royal Society of Chemistry (RSC)

Subject

Biochemistry, Genetics and Molecular Biology (miscellaneous),Molecular Biology,Biochemistry,Chemistry (miscellaneous)

Link

http://pubs.rsc.org/en/content/articlepdf/2022/CB/D2CB00108J

Reference43 articles.

1. Pushing the limits of targeted therapy in chronic myeloid leukaemia

2. Mechanisms of resistance to BCR-ABL and other kinase inhibitors

3. Targeting the SH2-Kinase Interface in Bcr-Abl Inhibits Leukemogenesis

4. Allosteric Inhibition of Bcr-Abl Kinase by High Affinity Monobody Inhibitors Directed to the Src Homology 2 (SH2)-Kinase Interface

5. The Human and Mouse Complement of SH2 Domain Proteins—Establishing the Boundaries of Phosphotyrosine Signaling

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