Assignment of IVL-Methyl side chain of the ligand-free monomeric human MALT1 paracaspase-IgL3 domain in solution.

Han X, Levkovets M, Lesovoy D, Sun R, Wallerstein J, Sandalova T, Agback T, Achour A, Agback P, Orekhov VY

Biomol NMR Assign 16 (2) 363-371 [2022-10-00; online 2022-09-12]

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-κB signalling pathway. Herein, we present the partial 1H, 13C Ile/Val/Leu-Methyl resonance assignment of the monomeric apo form of the paracaspase-IgL3 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).

Swedish NMR Centre (SNC) [Collaborative]

PubMed 36094731

DOI 10.1007/s12104-022-10105-3

Crossref 10.1007/s12104-022-10105-3

pmc: PMC9510110
pii: 10.1007/s12104-022-10105-3