title: Solution structure of the fifth repeat of factor H: a second example of the complement control protein module.
abstract: Modules which share the same consensus sequence are assumed to have common structural features, at the secondary and tertiary level. In order to test the extent of such similarities, it is necessary to examine the structures of several examples from each module family. Recently, the first three-dimensional structure of a complement control protein (CCP) module (the 16th repeat of human factor H, H16) was determined using a combination of two-dimensional NMR and simulated annealing [Norman, D.G., Barlow, P.N., Baron, M., Day, A.J., Sim, R.B., & Campbell, I.D. (1991) J. Mol. Biol. 219, 717-725]. Using the same techniques, the three-dimensional structure of a second CCP module (the 5th repeat of human factor H, H5) has now been determined. The primary sequence of H5 contains 17 residues which are identical and in equivalent position to those in H16. Thirteen of these 17 are part of the consensus sequence. The similarities between the secondary structure of H5 and that of H16 are extensive. This implies that the consensus sequence dictates a particular secondary structure. The tertiary structure of H5, a compact hydrophobic core wrapped in beta-strand and sheet, bears much overall resemblance to that of H16. However, there is a deletion in the first strand of H5, and an insertion in a loop, resulting in slightly shorter overall length. This is associated with a rearrangement of residues within the hydrophobic core. The side chain of the highly conserved Tyr29, which occupies a central position within the core of H16, lies on the periphery of the core of H5.
authors.affiliation: Department of Biochemistry, University of Oxford, U.K.
authors.forename: P N
authors.initials: PN
authors.lastname: Barlow
authors.forename: D G
authors.initials: DG
authors.lastname: Norman
authors.forename: A
authors.initials: A
authors.lastname: Steinkasserer
authors.forename: T J
authors.initials: TJ
authors.lastname: Horne
authors.forename: J
authors.initials: J
authors.lastname: Pearce
authors.forename: P C
authors.initials: PC
authors.lastname: Driscoll
authors.forename: R B
authors.initials: RB
authors.lastname: Sim
authors.forename: I D
authors.initials: ID
authors.lastname: Campbell
mesh_terms: D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D003180:Complement C3b Inactivator Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D017242:Complement Factor H; D004247:DNA / Q000235:genetics; D015870:Gene Expression; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D010957:Plasmids; D016133:Polymerase Chain Reaction; D011487:Protein Conformation; D012091:Repetitive Sequences, Nucleic Acid
chemical_list: C493495:CFH protein, human; D003180:Complement C3b Inactivator Proteins; D017242:Complement Factor H; D004247:DNA