Three-dimensional structure of a complement control protein module in solution - PubMed (original) (raw)
Three-dimensional structure of a complement control protein module in solution
D G Norman et al. J Mol Biol. 1991.
Abstract
The complement control protein (CCP) modules (also known as short consensus repeats) are defined by a consensus sequence within a stretch of about 60 amino acid residues. These modules have been identified more than 140 times in over 20 proteins, including 12 proteins of the complement system. The solution structure of the 16th CCP module from human complement factor H has been determined by a combination of 2-dimensional nuclear magnetic resonance spectroscopy and restrained simulated annealing. In all, 548 structurally important nuclear Overhauser enhancement cross-peaks were quantified as distance restraints and, together with 41 experimentally measured angle restraints, were incorporated into a simulated annealing protocol to determine a family of closely related structures that satisfied the experimental observations. The CCP structure is shown to be based on a beta-sandwich arrangement; one face made up of three beta-strands hydrogen-bonded to form a triple-stranded region at its centre and the other face formed from two separate beta-strands. Both faces of the molecule contribute highly conserved hydrophobic side-chains to a compact core. The regions between the beta-strands are composed of both well-defined turns and less well-defined loops. Analysis of CCP sequence alignments, in light of the determined structure, reveals a high degree of conservation amongst residues of obvious structural importance, while almost all insertions, deletions or replacements observed in the known sequences are found in the less well-defined loop regions. On the basis of these observations it is postulated that models of other CCP modules that are based on the structure presented here will be accurate. Certain families of CCP modules differ from the consensus in that they contain extra cysteine residues. As a test of structural consensus, the extra disulphide bridges are shown to be easily accommodated within the determined CCP model.
Similar articles
- Secondary structure of a complement control protein module by two-dimensional 1H NMR.
Barlow PN, Baron M, Norman DG, Day AJ, Willis AC, Sim RB, Campbell ID. Barlow PN, et al. Biochemistry. 1991 Jan 29;30(4):997-1004. doi: 10.1021/bi00218a016. Biochemistry. 1991. PMID: 1824927 - Solution structure of the fifth repeat of factor H: a second example of the complement control protein module.
Barlow PN, Norman DG, Steinkasserer A, Horne TJ, Pearce J, Driscoll PC, Sim RB, Campbell ID. Barlow PN, et al. Biochemistry. 1992 Apr 14;31(14):3626-34. doi: 10.1021/bi00129a011. Biochemistry. 1992. PMID: 1533152 - Oligomeric domain structure of human complement factor H by X-ray and neutron solution scattering.
Perkins SJ, Nealis AS, Sim RB. Perkins SJ, et al. Biochemistry. 1991 Mar 19;30(11):2847-57. doi: 10.1021/bi00225a017. Biochemistry. 1991. PMID: 1826087 - Translational mini-review series on complement factor H: structural and functional correlations for factor H.
Schmidt CQ, Herbert AP, Hocking HG, Uhrín D, Barlow PN. Schmidt CQ, et al. Clin Exp Immunol. 2008 Jan;151(1):14-24. doi: 10.1111/j.1365-2249.2007.03553.x. Clin Exp Immunol. 2008. PMID: 18081691 Free PMC article. Review. - Structure and flexibility of the multiple domain proteins that regulate complement activation.
Kirkitadze MD, Barlow PN. Kirkitadze MD, et al. Immunol Rev. 2001 Apr;180:146-61. doi: 10.1034/j.1600-065x.2001.1800113.x. Immunol Rev. 2001. PMID: 11414356 Review.
Cited by
- Overview of protein structural and functional folds.
Sun PD, Foster CE, Boyington JC. Sun PD, et al. Curr Protoc Protein Sci. 2004 May;Chapter 17(1):Unit 17.1. doi: 10.1002/0471140864.ps1701s35. Curr Protoc Protein Sci. 2004. PMID: 18429251 Free PMC article. Review. - Identification of Potential Novel Interacting Partners for Coagulation Factor XIII B (FXIII-B) Subunit, a Protein Associated with a Rare Bleeding Disorder.
Singh S, Akhter MS, Dodt J, Volkers P, Reuter A, Reinhart C, Krettler C, Oldenburg J, Biswas A. Singh S, et al. Int J Mol Sci. 2019 May 31;20(11):2682. doi: 10.3390/ijms20112682. Int J Mol Sci. 2019. PMID: 31159152 Free PMC article. - In-depth proteomic analysis of shell matrix proteins of Pinctada fucata.
Liu C, Li S, Kong J, Liu Y, Wang T, Xie L, Zhang R. Liu C, et al. Sci Rep. 2015 Nov 26;5:17269. doi: 10.1038/srep17269. Sci Rep. 2015. PMID: 26608573 Free PMC article. - Evolution of the complement system: from defense of the single cell to guardian of the intravascular space.
Elvington M, Liszewski MK, Atkinson JP. Elvington M, et al. Immunol Rev. 2016 Nov;274(1):9-15. doi: 10.1111/imr.12474. Immunol Rev. 2016. PMID: 27782327 Free PMC article. Review. - Estimation of interdomain flexibility of N-terminus of factor H using residual dipolar couplings.
Maciejewski M, Tjandra N, Barlow PN. Maciejewski M, et al. Biochemistry. 2011 Sep 27;50(38):8138-49. doi: 10.1021/bi200575b. Epub 2011 Aug 31. Biochemistry. 2011. PMID: 21793561 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
Research Materials
Miscellaneous