Disease-linked mutations in factor H reveal pivotal role of cofactor activity in Self-surface–selective regulation of complement activation

• Main Authors: Kerr, H, Wong, E, Makou, E, Yang, Y, Marchbank, K, Kavanagh, D, Richards, A, Herbert, A.P, Barlow, P.N
• Other Authors: MEDICINE
• Format: Article
• Published: American Society for Biochemistry and Molecular Biology Inc. 2020
• Subjects: Bins; Blood; Chemical activation; Proteins; Age-related macular degeneration; Cofactor activity; Complement activations; Complement control proteins; Complement systems; Sheep erythrocytes; Streptococcus pneumoniae; Surface selectivity; Disease control; complement component C3b; complement component C3d; complement factor H; sialic acid; alternative complement pathway C3 C5 convertase; bacterial protein; CFI protein, human; complement factor H, human; complement factor I; hybrid protein; immobilized protein; peptide fragment; amino acid substitution; amino terminal sequence; animal cell; Article; binding affinity; binding site; biological activity; carboxy terminal sequence; CCP 1 gene; complement activation; complement mediated hemolysis; controlled study; decay accelerating activity; disease linked mutation; erythrocyte; factor I cofactor activity; gene; gene mutation; genetic association; hemolysis; hemolytic uremic syndrome; Komagataella pastoris; nonhuman; priority journal; protein cross linking; protein domain; protein function; protein synthesis; regulatory mechanism; self surface selective regulation; sheep; structure activity relation; surface property; animal; chemistry; comparative study; domestic sheep; genetics; human; macular degeneration; metabolism; mutation; solubility; Amino Acid Substitution; Animals; Atypical Hemolytic Uremic Syndrome; Bacterial Proteins; Binding Sites; Complement Activation; Complement C3 Convertase, Alternative Pathway; Complement C3d; Complement Factor H; Complement Factor I; Erythrocytes; Hemolysis; Humans; Immobilized Proteins; Macular Degeneration; Mutation; Peptide Fragments; Protein Interaction Domains and Motifs; Recombinant Fusion Proteins; Sheep, Domestic; Solubility; Surface Properties
• Online Access: https://scholarbank.nus.edu.sg/handle/10635/179259
• Institution: National University of Singapore

10.1074/jbc.M117.795088