TY - JOUR
T1 - Co-operativity between modules within a C3b-binding site of complement receptor type 1
AU - Kirkitadze, M. D.
AU - Dryden, D. T.F.
AU - Kelly, Sharon M.
AU - Price, Nicholas C.
AU - Wang, X.
AU - Krych, M.
AU - Atkinson, J. P.
AU - Barlow, P. N.
N1 - Funding Information:
M.D.K. is funded by the Human Frontiers Science program. D.T.F.D. is funded by Royal Society of Great Britain. This work was also funded by the Edinburgh Centre for Protein Technology. The Circular Dichroism facility in Stirling University is funded by BBSRC. Work in St. Louis was supported in part by funding from the National Institute of Health (R01 AI41592) and from CytoMed Inc. (Cambridge, MA). J.P.A. and Washington University have a financial interest in CytoMed Inc.
PY - 1999/10/1
Y1 - 1999/10/1
N2 - 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.
AB - 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.
KW - CR1
KW - Complement
KW - Differential scanning calorimetry
KW - Fluorescence
KW - Module
KW - Protein folding
UR - https://www.scopus.com/pages/publications/0032832221
U2 - 10.1016/S0014-5793(99)01205-3
DO - 10.1016/S0014-5793(99)01205-3
M3 - Article
C2 - 10508932
AN - SCOPUS:0032832221
SN - 0014-5793
VL - 459
SP - 133
EP - 138
JO - FEBS Letters
JF - FEBS Letters
IS - 1
ER -