Insights into mechanisms of MALT1 allostery from NMR and AlphaFold dynamic analyses.

ABSTRACT: Mucosa-associated lymphoid tissue lymphoma-translocation protein 1 (MALT1) is an attractive target for the development of modulatory compounds in the treatment of lymphoma and other cancers. While the three-dimensional structure of MALT1 has been previously determined through X-ray analysis, its dynamic behaviour in solution has remained unexplored. We present here dynamic analyses of the apo MALT1 form along with the E549A mutation. This investigation used NMR ¹⁵N relaxation and NOE measurements between side-chain methyl groups. Our findings confirm that MALT1 exists as a monomer in solution, and demonstrate that the domains display semi-independent movements in relation to each other. Our dynamic study, covering multiple time scales, along with the assessment of conformational

SUBMITTER: Wallerstein J 

PROVIDER: S-EPMC11252132 | biostudies-literature | 2024 Jul

REPOSITORIES: biostudies-literature