1NT0

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

Summary for 1NT0

• Entry DOI: 10.2210/pdb1nt0/pdb
• Descriptor: mannose-binding protein associated serine protease-2, 2-acetamido-2-deoxy-beta-D-glucopyranose, CALCIUM ION, ... (5 entities in total)
• Functional Keywords: mannose-binding protein, masp, cub domain, egf like domain., hydrolase, sugar binding protein
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Secreted: Q9JJS8
• Total number of polymer chains: 2
• Total formula weight: 65758.78

Authors

Feinberg, H.,Uitdehaag, J.C.M.,Davies, J.M.,Wallis, R.,Drickamer, K.,Weis, W.I. (deposition date: 2003-01-28, release date: 2003-05-20, Last modification date: 2025-03-26)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.7 Å)