Journal
PLOS ONE
Volume 6, Issue 9, Pages -Publisher
PUBLIC LIBRARY SCIENCE
DOI: 10.1371/journal.pone.0023220
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Funding
- Canadian Institutes for Health Research [1097737]
- Canada Foundation for Innovation
- Genome Canada through the Ontario Genomics Institute
- GlaxoSmithKline
- Karolinska Institutet
- Knut and Alice Wallenberg Foundation
- Ontario Innovation Trust
- Ontario Ministry for Research and Innovation
- Merck Co., Inc.
- Novartis Research Foundation
- Swedish Agency for Innovation
- Swedish Foundation for Strategic Research
- Wellcome Trust
- United States Department of Energy, Office of Science, Office of Basic Energy Sciences [DE-AC02-06CH11357]
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Background: Mucosa-associated lymphoid tissue 1 (MALT1) plays an important role in the adaptive immune program. During TCR- or BCR-induced NF-kappa B activation, MALT1 serves to mediate the activation of the IKK (I kappa B kinase) complex, which subsequently regulates the activation of NF-kappa B. Aggregation of MALT1 is important for E3 ligase activation and NF-kappa B signaling. Principal Findings: Unlike the isolated CARD or paracaspase domains, which behave as monomers, the tandem Ig-like domains of MALT1 exists as a mixture of dimer and tetramer in solution. High-resolution structures reveals a protein-protein interface that is stabilized by a buried surface area of 1256 angstrom(2) and contains numerous hydrogen and salt bonds. In conjunction with a second interface, these interactions may represent the basis of MALT1 oligomerization. Conclusions: The crystal structure of the tandem Ig-like domains reveals the oligomerization potential of MALT1 and a potential intermediate in the activation of the adaptive inflammatory pathway.
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