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

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

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Abstract

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. Copyright (C) 1999 Federation of European Biochemical Societies.

Original languageEnglish
Pages (from-to)133-138
Number of pages6
JournalFEBS Letters
Volume459
Issue number1
DOIs
StatePublished - Oct 1 1999

Keywords

  • CR1
  • Complement
  • Differential scanning calorimetry
  • Fluorescence
  • Module
  • Protein folding

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    Kirkitadze, M. D., Dryden, D. T. F., Kelly, S. M., Price, N. C., Wang, X., Krych, M., Atkinson, J. P., & Barlow, P. N. (1999). Co-operativity between modules within a C3b-binding site of complement receptor type 1. FEBS Letters, 459(1), 133-138. https://doi.org/10.1016/S0014-5793(99)01205-3