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BRENDA support

Literature summary for 3.4.21.41 extracted from

  • Budayova-Spano, M.; Grabarse, W.; Thielens, N.M.; Hillen, H.; Lacroix, M.; Schmidt, M.; Fontecilla-Camps, J.C.; Arlaud, G.J.; Gaboriaud, C.
    Monomeric structures of the zymogen and active catalytic domain of complement protease C1r: further insights into the C1 activation mechanism (2002), Structure, 10, 1509-1519.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapour diffusion method, 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 Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P00736
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