Co‐operativity between modules within a C3b‐binding site of complement receptor type 1

FEBS Letters

Kirkitadze, M.D.²  Price, Nicholas C.³  Dryden, D.T.F.⁴  Atkinson, J.P.¹  Wang, X.¹  Krych, M.¹  Barlow, P.N.²  Kelly, Sharon M.³ 

[1] Department of Internal Medicine, Division of Rheumatology, Washington University School of Medicine, 660 S. Euclid, Box 8045, St. Louis, MO 63110, USA;The Edinburgh Centre for Protein Technology, Department of Chemistry, University of Edinburgh, West Mains Road, Edinburgh EH9 3JJ, UK;Department of Biological Sciences, University of Stirling, Stirling FK9 4LA, UK;Institute of Cell and Molecular Biology, University of Edinburgh, West Mains Road, Edinburgh EH9 3JR, UK

关键词: CR1;    Complement;    Module;    Protein folding;    Differential scanning calorimetry;    Fluorescence;    CR1;    complement receptor type 1;    CR1∼16;    17;    etc.;    16th and 17th modules etc. of CR1;    DSC;    differential scanning calorimetry;    CD;    circular dichroism;    NMR;    nuclear magnetic resonance;    HSQC;    heteronuclear single quantum coherence;    VCP;    Vaccinia virus complement control protein;    GdmCl;    guanidinium chloride;    ΔH cal;    calorimetric enthalpy;   

DOI  :  10.1016/S0014-5793(99)01205-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Complement receptor type 1 (CR1) has 30 modules in its extracellular portion. An understanding of structure-function relationships within CR1 is being assembled gradually from studies of overlapping protein fragments. A CR1 fragment corresponding to modules 16 and 17 was expressed recombinantly as a non-glycosylated protein and its stability and unfolding characteristics studied using biophysical techniques. The results were compared with data collected previously on a CR1 fragment encompassing modules 15, 16 and 17 which together constitute a C3b-binding site (Kirkitadze, M.D., Krych, M., Uhrin, D., Dryden, D.T.F., Smith, B.O., Wang, X., Hauhart, R., Atkinson, J.P. and Barlow, P.N. (1999) Biochemistry 38, 7019–7031). Modules within CR1 were found to co-operate during unfolding. The folding, stability and flexibility of this protein is therefore likely to be a complex function, and not just the sum, of contributions from individual modules.

【 授权许可】

Unknown