Effects of cyclic GMP on the secondary structure of cyclic GMP dependent protein kinase and an analysis of the enzymes and amino-terminal domain by far-ultraviolet circular dichroism
- 30 September 1990
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 29 (42), 9921-9928
- https://doi.org/10.1021/bi00494a024
Abstract
Far-UV circular dichroism spectra of bovine lung cyclic GMP dependent protein kinase (G-kinase) show that the enzyme contains .alpha.-helical and .beta.-pleated sheet elements. Binding of cyclic GMP changes the spectra in a way consistent with the induction of .beta.-sheet from random coil. Examination of the amino-terminal sequence of G-kinase indicates the presence of a strongly .alpha.-helical segment with several features in common with the leucine zipper motif. We propose that this sequence may be the important part of the dimerization domain of the enzyme. A synthetic peptide corresponding to amino acids 1-39 of G-kinase has a strongly .alpha.-helical CD spectrum, supporting the predicted secondary structure of this amino-terminal sequence. In contrast to the native enzyme, a structure reduced in .alpha.-helix was found when a constitutively active form of G-kinase, which lacks amino acids 1-77, was studied.Keywords
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