Structural Genomics Consortium, University of Toronto, Toronto, Ontario, Canada.
PLoS One. 2011;6(9):e23220. doi: 10.1371/journal.pone.0023220. Epub 2011 Sep 23.
Mucosa-associated lymphoid tissue 1 (MALT1) plays an important role in the adaptive immune program. During TCR- or BCR-induced NF-κB activation, MALT1 serves to mediate the activation of the IKK (IκB kinase) complex, which subsequently regulates the activation of NF-κB. Aggregation of MALT1 is important for E3 ligase activation and NF-κB signaling.
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 Å(2) and contains numerous hydrogen and salt bonds. In conjunction with a second interface, these interactions may represent the basis of MALT1 oligomerization.
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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黏膜相关淋巴组织 1（MALT1）在适应性免疫计划中发挥着重要作用。在 TCR 或 BCR 诱导的 NF-κB 激活过程中，MALT1 作为 IKK（IκB 激酶）复合物的激活剂，调节 NF-κB 的激活。MALT1 的聚集对于 E3 连接酶的激活和 NF-κB 信号转导很重要。
与单体行为的分离 CARD 或 paracaspase 结构域不同，MALT1 的串联 Ig 样结构域在溶液中以二聚体和四聚体的混合物形式存在。高分辨率结构揭示了一个由 1256 Ų 的埋藏表面积稳定的蛋白-蛋白界面，并包含许多氢键和盐键。与第二个界面结合，这些相互作用可能代表 MALT1 寡聚化的基础。
串联 Ig 样结构域的晶体结构揭示了 MALT1 的寡聚化潜力和适应性炎症途径激活的潜在中间产物。
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