Effect of Zinc and Temperature on The Conformation of The γ Subunit of Retinal Phosphodiesterase:  A Natively Unfolded Protein

Authors

Vladimir N. Uversky, University of California, Santa CruzFollow
Sergei E. Permyakov, Institute for Biological Instrumentation of the Russian Academy of Sciences
Vasily E. Zagranichny, Branch of M. M. Shemyakin and Yu. A. Ovchinnikov Institute ofBioorganic Chemistry of the Russian Academy of Sciences

Document Type

Article

Publication Date

2002

Keywords

Cyclic GMP Phosphodiesterase, Signal Transduction, Intrinsically Unordered Protein, Conformational Transition, Partially Folded Intermediat

Digital Object Identifier (DOI)

https://doi.org/10.1021/pr0155127

Abstract

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.

Was this content written or created while at USF?

Yes

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.
https://digitalcommons.usf.edu/mme_facpub/690