1nt0

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spinqualitylabelsall models 1nt0, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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

Overview

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.

About this Structure

1NT0 is a Single protein structure of sequence from Rattus norvegicus with NAG, CA and EDO as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of the CUB1-EGF-CUB2 region of mannose-binding protein associated serine protease-2., Feinberg H, Uitdehaag JC, Davies JM, Wallis R, Drickamer K, Weis WI, EMBO J. 2003 May 15;22(10):2348-59. PMID:12743029

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