1elv
From Proteopedia
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CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN COMPLEMENT C1S PROTEASE
Overview
C1s is the highly specific modular serine protease that mediates the, proteolytic activity of the C1 complex and thereby triggers activation of, the complement cascade. The crystal structure of a catalytic fragment from, human C1s comprising the second complement control protein (CCP2) module, and the chymotrypsin-like serine protease (SP) domain has been determined, and refined to 1.7 A resolution. In the areas surrounding the active site, the SP structure reveals a restricted access to subsidiary substrate, binding sites that could be responsible for the narrow specificity of C1s., The ellipsoidal CCP2 module is oriented perpendicularly to the surface of, the SP domain. This arrangement is maintained through a rigid, module-domain interface involving intertwined proline- and ... [(full description)]
About this Structure
1ELV is a [Single protein] structure of sequence from [Homo sapiens] with SO4 and NES as [ligands]. Active as [Complement subcomponent C1s], with EC number [3.4.21.42]. Structure known Active Site: CAT. Full crystallographic information is available from [OCA].
Reference
Crystal structure of the catalytic domain of human complement c1s: a serine protease with a handle., Gaboriaud C, Rossi V, Bally I, Arlaud GJ, Fontecilla-Camps JC, EMBO J. 2000 Apr 17;19(8):1755-65. PMID:10775260
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