1NT0

Crystal structure of the CUB1-EGF-CUB2 region of MASP2

1NT0 の概要

• エントリーDOI: 10.2210/pdb1nt0/pdb
• 分子名称: mannose-binding protein associated serine protease-2, 2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: mannose-binding protein, masp, cub domain, egf like domain., hydrolase, sugar binding protein
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Secreted: Q9JJS8
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 65758.78

構造登録者

Feinberg, H.,Uitdehaag, J.C.M.,Davies, J.M.,Wallis, R.,Drickamer, K.,Weis, W.I. (登録日: 2003-01-28, 公開日: 2003-05-20, 最終更新日: 2025-03-26)

主引用文献

Feinberg, H.,Uitdehaag, J.C.M.,Davies, J.M.,Wallis, R.,Drickamer, K.,Weis, W.I.
Crystal structure of the CUB1-EGF-CUB2 region of mannose-binding protein associated serine protease-2
Embo J., 22:2348-2359, 2003

PubMed Abstract: Serum mannose-binding proteins (MBPs) are C-type lectins that recognize cell surface carbohydrate structures on pathogens, and trigger killing of these targets by activating the complement pathway. MBPs circulate as a complex with MBP-associated serine proteases (MASPs), which become activated upon engagement of a target cell surface. The minimal functional unit for complement activation is a MASP homodimer bound to two MBP trimeric subunits. MASPs have a modular structure consisting of an N-terminal CUB domain, a Ca(2+)-binding EGF-like domain, a second CUB domain, two complement control protein modules and a C-terminal serine protease domain. The CUB1-EGF-CUB2 region mediates homodimerization and binding to MBP. The crystal structure of the MASP-2 CUB1-EGF-CUB2 dimer reveals an elongated structure with a prominent concave surface that is proposed to be the MBP-binding site. A model of the full six-domain structure and its interaction with MBPs suggests mechanisms by which binding to a target cell transmits conformational changes from MBP to MASP that allow activation of its protease activity.

PubMed: 12743029
DOI: 10.1093/emboj/cdg236

実験手法

X-RAY DIFFRACTION (2.7 Å)