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

• 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).

Subject headings

NATURVETENSKAP  -- Biologi -- Biofysik (hsv//swe)

NATURAL SCIENCES  -- Biological Sciences -- Biophysics (hsv//eng)

MEDICIN OCH HÄLSOVETENSKAP  -- Medicinsk bioteknologi -- Medicinsk bioteknologi (hsv//swe)

MEDICAL AND HEALTH SCIENCES  -- Medical Biotechnology -- Medical Biotechnology (hsv//eng)

Keyword

MALT1

Paracaspase

H-1

C-13 Ile

Val

Leu-Methyl resonance

t-cell

nmr-spectroscopy

protease activity

activation

lymphoma

proteins

trosy

relaxation

responses

complex

Biophysics

Spectroscopy

Publication and Content Type

ref (subject category)

art (subject category)