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

Xiao Han, Maria Levkovets, Dmitry Lesovoy, Renhua Sun, Johan Wallerstein, Tatyana Sandalova, Tatyana Agback, Adnane Achour, Peter Agback, Vladislav Yu. Orekhov

Research output: Contribution to journalArticlepeer-review

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-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).
Original languageEnglish
Pages (from-to)363-371
Number of pages9
JournalBiomolecular NMR Assignments
Volume16
DOIs
Publication statusPublished - 2022 Sept 12
Externally publishedYes

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