Co-operativity between modules within a C3b-binding site of complement receptor type 1.
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.
Kirkitadze
M D
MD
The Edinburgh Centre for Protein Technology, Department of Chemistry, University of Edinburgh, West Mains Road, Edinburgh, UK.
Dryden
D T
DT
Kelly
S M
SM
Price
N C
NC
Wang
X
X
Krych
M
M
Atkinson
J P
JP
Barlow
P N
PN
D001665:Binding Sites; D002152:Calorimetry, Differential Scanning; D002942:Circular Dichroism; D003179:Complement C3b / Q000737:chemistry / Q000378:metabolism*; D019791:Guanidine / Q000494:pharmacology; D009682:Magnetic Resonance Spectroscopy; D010843:Pichia; D011487:Protein Conformation; D017510:Protein Folding; D011951:Receptors, Complement / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D013050:Spectrometry, Fluorescence
D011951:Receptors, Complement; D003179:Complement C3b; D019791:Guanidine