کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8472158 | 1550303 | 2007 | 10 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Assembly of C1 and the MBL- and ficolin-MASP complexes: Structural insights
دانلود مقاله + سفارش ترجمه
دانلود مقاله ISI انگلیسی
رایگان برای ایرانیان
کلمات کلیدی
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
بیولوژی سلول
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
The classical pathway C1 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 (C1q, MBL, L-, H- or M-ficolin), and a protease component, which is either a tetramer (C1s-C1r-C1r-C1s) or a dimer ((MASP)2). Recent functional and 3-D structural investigations have revealed that C1r/C1s and the MASPs associate through a common mechanism involving their N-terminal CUB1-EGF region. In contrast, the C1s-C1r-C1r-C1s 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.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Immunobiology - Volume 212, Issues 4â5, 26 June 2007, Pages 279-288
Journal: Immunobiology - Volume 212, Issues 4â5, 26 June 2007, Pages 279-288
نویسندگان
Christine Gaboriaud, Florence Teillet, Lynn A. Gregory, Nicole M. Thielens, Gérard J. Arlaud,