Effect of Zinc and Temperature on The Conformation of The γ Subunit of Retinal Phosphodiesterase: A Natively Unfolded Protein
Cyclic GMP Phosphodiesterase, Signal Transduction, Intrinsically Unordered Protein, Conformational Transition, Partially Folded Intermediat
Digital Object Identifier (DOI)
The cyclic GMP phosphodiesterase γ-subunit (PDEγ) 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 PDEγ has a high-affinity zinc-binding site (Kd ∼1 μM), 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 PDEγ are discussed.
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Citation / Publisher Attribution
Journal of Proteome Research, v. 1, issue 2, p. 149-159
Scholar Commons Citation
Uversky, Vladimir N.; Permyakov, Sergei E.; and Zagranichny, Vasily E., "Effect of Zinc and Temperature on The Conformation of The γ Subunit of Retinal Phosphodiesterase: A Natively Unfolded Protein" (2002). Molecular Medicine Faculty Publications. 690.