3v4l | pdb_00003v4l

Mouse MALT1(caspase-IG3 domains) in complex with a irreversible peptidic inhibitor

spinqualitylabelsall models 3v4l, resolution 3.15Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3v4l is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.15Å Ligands: CF0, PHQ, PRD_001076 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function MALT1_MOUSE Enhances BCL10-induced activation of NF-kappa-B. Involved in nuclear export of BCL10. Binds to TRAF6, inducing TRAF6 oligomerization and activation of its ligase activity. Has ubiquitin ligase activity (By similarity). MALT1-dependent BCL10 cleavage plays an important role in T-cell antigen receptor-induced integrin adhesion (By similarity).[UniProtKB:Q9UDY8] Publication Abstract from PubMed The formation of the CBM (CARD11-BCL10-MALT1) complex is pivotal for antigen-receptor-mediated activation of the transcription factor NF-kappaB. Signaling is dependent on MALT1 (mucosa-associated lymphoid tissue lymphoma translocation protein 1), which not only acts as a scaffolding protein but also possesses proteolytic activity mediated by its caspase-like domain. It remained unclear how the CBM activates MALT1. Here, we provide biochemical and structural evidence that MALT1 activation is dependent on its dimerization and show that mutations at the dimer interface abrogate activity in cells. The unliganded protease presents itself in a dimeric yet inactive state and undergoes substantial conformational changes upon substrate binding. These structural changes also affect the conformation of the C-terminal Ig-like domain, a domain that is required for MALT1 activity. Binding to the active site is coupled to a relative movement of caspase and Ig-like domains. MALT1 binding partners thus may have the potential of tuning MALT1 protease activity without binding directly to the caspase domain. Structural Determinants of MALT1 Protease Activity.,Wiesmann C, Leder L, Blank J, Bernardi A, Melkko S, Decock A, D'Arcy A, Villard F, Erbel P, Hughes N, Freuler F, Nikolay R, Alves J, Bornancin F, Renatus M J Mol Biol. 2012 Feb 23. PMID:22366302 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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