Abstract:
:Phosphorylation of the regulatory (R) domain initiates cystic fibrosis transmembrane conductance regulator (CFTR) Cl(-) channel activity. To discover how the function of this domain is determined by its structure, we produced an R domain protein (R8) that spanned residues 708-831 of CFTR. Phosphorylated, but not unphosphorylated, R8 stimulated activity of CFTR channels lacking this domain, indicating that R8 is functional. Unexpectedly, this functional R8 was predominantly random coil, as revealed by CD and limited proteolysis. The CD spectra of both phosphorylated and nonphosphorylated R8 were similar in aqueous buffer. The folding agent trimethylamine N-oxide induced only a small increase in the helical content of nonphosphorylated R8 and even less change in the helical content of phosphorylated R8. These data, indicating that the R domain is predominantly random coil, may explain the seemingly complex way in which phosphorylation regulates CFTR channel activity.
journal_name
Proc Natl Acad Sci U S Aauthors
Ostedgaard LS,Baldursson O,Vermeer DW,Welsh MJ,Robertson ADdoi
10.1073/pnas.100588797keywords:
subject
Has Abstractpub_date
2000-05-09 00:00:00pages
5657-62issue
10eissn
0027-8424issn
1091-6490pii
100588797journal_volume
97pub_type
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