1md7

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spinqualitylabelsall models 1md7, resolution 3.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Monomeric structure of the zymogen of complement protease C1r

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

C1r is the serine protease (SP) that mediates autoactivation of C1, the, complex that triggers the classical complement pathway. We have determined, the crystal structure of two fragments from the human C1r catalytic, domain, each encompassing the second complement control protein (CCP2), module and the SP domain. The wild-type species has an active structure, whereas the S637A mutant is a zymogen. The structures reveal a restricted, hinge flexibility of the CCP2-SP interface, and both are characterized by, the unique alpha-helical conformation of loop E. The zymogen activation, domain exhibits high mobility, and the active structure shows a restricted, access to most substrate binding subsites. Further implications relevant, to the C1r self-activation process are derived from protein-protein, interactions in the crystals.

Disease

Known disease associated with this structure: C1r/C1s deficiency, combined OMIM:[216950]

About this Structure

1MD7 is a Single protein structure of sequence from Homo sapiens with NDG as ligand. Active as Complement subcomponent C1r, with EC number 3.4.21.41 Full crystallographic information is available from OCA.

Reference

Monomeric structures of the zymogen and active catalytic domain of complement protease c1r: further insights into the c1 activation mechanism., Budayova-Spano M, Grabarse W, Thielens NM, Hillen H, Lacroix M, Schmidt M, Fontecilla-Camps JC, Arlaud GJ, Gaboriaud C, Structure. 2002 Nov;10(11):1509-19. PMID:12429092

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