Structure of Human Complement Factor H Carboxyl Terminal Domains 19-20: a Basis for Atypical Hemolytic Uremic Syndrome
Structure of complement factor H carboxyl-terminus reveals molecular basis of atypical haemolytic uremic syndrome.
GKCGPPPPIDNGDITSFPLSVYAPASSVEYQCQNLYQLEGNKRITCRNGQWSEPPKCLHPCVISREIMENYNIALRWTAK QKLYSRTGESVEFVCKRGYRLSSRSHTLRTTCWDGKLEYPTCAKR
Before crystallization the protein was concentrated to 10 mg/ml and dialysed into 20 mM Tris, 50 mM NaCl, pH 7.0. The protein was crystallized in sitting drops by mixing 1 ul of protein solution at 10 mg/ml with 1 ul of reservoir solution of 2.2 M (NH4)2SO4, 0.1 M Tris-HCl, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 298.0K
HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
Crystal packing of FH19-20 in the asymmetric unit reveals tightly packed tetrameric assembly of domains of FH19-20; may have biological relevance
Sushi (CCP/SCR) domain, Complement, Regulator, Factor H, Beta-1H Globulin, Immune system, Atypical Hemolytic Uremic Syndrome, Heparin Binding