Assignment of IVL-Methyl side chain of the ligand-free monomeric human MALT1 paracaspase-IgL(3) domain in solution

Abstract

Mucosa-associated lymphoid tissue protein 1 (MALT1) plays a key role in adaptive immune responses by modulating specific intracellular signalling pathways that control the development and proliferation of both T and B cells. Dysfunction of these pathways is coupled to the progress of highly aggressive lymphoma as well as to potential development of an array of different immune disorders. In contrast to other signalling mediators, MALT1 is not only activated through the formation of the CBM complex together with the proteins CARMA1 and Bcl10, but also by acting as a protease that cleaves multiple substrates to promote lymphocyte proliferation and survival via the NF-kappa B signalling pathway. Herein, we present the partial H-1, C-13 Ile/Val/Leu-Methyl resonance assignment of the monomeric apo form of the paracaspase-IgL(3) domain of human MALT1. Our results provide a solid ground for future elucidation of both the three-dimensional structure and the dynamics of MALT1, key for adequate development of inhibitors, and a thorough molecular understanding of its function(s).

Keywords

MALT1; Paracaspase; H-1; C-13 Ile; Val; Leu-Methyl resonance

Published in

Biomolecular NMR Assignments
2022, Publisher: SPRINGER

SLU Authors

• Agback, Tatiana

  • Department of Molecular Sciences, Swedish University of Agricultural Sciences
    

• Agback, Peter

  • Department of Molecular Sciences, Swedish University of Agricultural Sciences
    

UKÄ Subject classification

Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)


Publication identifier

DOI: https://doi.org/10.1007/s12104-022-10105-3

Permanent link to this page (URI)

https://res.slu.se/id/publ/119078