Effect of Zinc and Temperature on the Conformation of the γ Subunit of Retinal Phosphodiesterase: A Natively Unfolded Protein
Journal of Proteome Research2002Vol. 1(2), pp. 149–159
Citations Over TimeTop 15% of 2002 papers
Vladimir N. Uversky, Sergei E. Permyakov, Vasily E. Zagranichny, I. L. Rodionov, Anthony L. Fink, Alexandra M. Cherskaya, and Lyubov A.Wasserman, Eugene A. Permyakov
Abstract
The cyclic GMP phosphodiesterase gamma-subunit (PDEgamma) was shown to belong to the family of natively unfolded proteins. Increasing temperature transforms the protein into a more ordered (but still relatively disordered) conformation. The C-terminal part of PDEgamma has a high-affinity zinc-binding site (Kd approximately 1 microM), with His75 and His79 being directly involved into the coordination of Zn2+. Zinc-loaded protein remains effectively unfolded. Possible implications of these findings to the functioning of PDEgamma are discussed.
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