Assembly of C1 and the MBL- and ficolin-MASP complexes: Structural insights
Assembly of C1 and the MBL- and ficolin-MASP complexes: Structural insights
复制标题
DOI：
10.1016/j.imbio.2006.11.007
复制
发表时间：
2007-01-01
期刊：
影响因子：
2.8
通讯作者：
Arlaud, Gerard J.
中科院分区：
文献类型：
--
作者：
Gaboriaud, Christine;Teillet, Florence;Arlaud, Gerard J.
参与凝集素途径活化的经典途径Cl复合物和MBL-MASP和纤维胶凝蛋白-MASP复合物具有几个共同特征。两种类型的复合物都由两个亚基组装：寡聚识别蛋白（Clq、MBL、L-、H-或M-纤维胶凝蛋白）和蛋白酶组分，其是四聚体（Cls-Clr-Clr-Cls）或二聚体（（MASP）2）。最近的功能和3-D结构研究表明，Clr/Cls和MASPs通过涉及其N-末端CUBI-EGF区域的共同机制相关联。相比之下，Cls-Clr-Clr-Cls四聚体和（MASP）2二聚体似乎已经进化出不同的策略来与它们的伴侣蛋白缔合。本文的目的是回顾这些最新进展。(c)2006年Elsevier GmbH。All rights reserved.
The classical pathway C I complex, and the MBL-MASP and ficolin-MASP complexes involved in activation of the lectin pathway have several features in common. Both types of complexes are assembled from two subunits: an oligomeric recognition protein (Clq, MBL, L-, H- or M-ficolin), and a protease component, which is either a tetramer (Cls-Clr-Clr-Cls) or a dimer ((MASP)2). Recent functional and 3-D structural investigations have revealed that Clr/Cls and the MASPs associate through a common mechanism involving their N-terminal CUBI-EGF region. In contrast, the Cls-Clr-Clr-Cls tetramer and the (MASP)2 dimers appear to have evolved distinct strategies to associate with their partner proteins. The purpose of this article is to review these recent advances. (c) 2006 Elsevier GmbH. All rights reserved.