3V55

Human MALT1 (334-719) in its ligand free form

3V55 の概要

• エントリーDOI: 10.2210/pdb3v55/pdb
• 関連するPDBエントリー: 3V4L 3V4O
• 分子名称: Mucosa-associated lymphoid tissue lymphoma translocation protein 1 (2 entities in total)
• 機能のキーワード: caspase, ig domain, hydrolase, traf6, bcl10, cytosol
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Cytoplasm, perinuclear region : Q9UDY8
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 43983.51

構造登録者

Renatus, M.,Wiesmann, C. (登録日: 2011-12-16, 公開日: 2012-03-14, 最終更新日: 2023-11-29)

主引用文献

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.
Structural Determinants of MALT1 Protease Activity.
J.Mol.Biol., 419:4-21, 2012

PubMed Abstract: The formation of the CBM (CARD11-BCL10-MALT1) complex is pivotal for antigen-receptor-mediated activation of the transcription factor NF-κB. 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.

PubMed: 22366302
DOI: 10.1016/j.jmb.2012.02.018

実験手法

X-RAY DIFFRACTION (1.81 Å)