1gpz
From Proteopedia
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THE CRYSTAL STRUCTURE OF THE ZYMOGEN CATALYTIC DOMAIN OF COMPLEMENT PROTEASE C1R
Overview
C1r is the modular serine protease (SP) that mediates autolytic activation, of C1, the macromolecular complex that triggers the classical pathway of, complement. The crystal structure of a mutated, proenzyme form of the, catalytic domain of human C1r, comprising the first and second complement, control protein modules (CCP1, CCP2) and the SP domain has been solved and, refined to 2.9 A resolution. The domain associates as a homodimer with an, elongated head-to-tail structure featuring a central opening and involving, interactions between the CCP1 module of one monomer and the SP domain of, its counterpart. Consequently, the catalytic site of one monomer and the, cleavage site of the other are located at opposite ends of the dimer. The, structure reveals unusual features in the SP domain ... [(full description)]
About this Structure
1GPZ is a [Single protein] structure of sequence from [Homo sapiens] with NAG as [ligand]. Full crystallographic information is available from [OCA].
Reference
The crystal structure of the zymogen catalytic domain of complement protease C1r reveals that a disruptive mechanical stress is required to trigger activation of the C1 complex., Budayova-Spano M, Lacroix M, Thielens NM, Arlaud GJ, Fontecilla-Camps JC, Gaboriaud C, EMBO J. 2002 Feb 1;21(3):231-9. PMID:11823416
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