Effect of Zinc and Temperature on the Conformation of the γ Subunit of Retinal Phosphodiesterase: A Natively Unfolded Protein
| Autor: | Alexandra M. Cherskaya, Vladimir N. Uversky, Vasily E Zagranichny, Anthony L. Fink, Igor L Rodionov, Lyubov A Wasserman, Sergey E Permyakov, Eugene A Permyakov |
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| Rok vydání: | 2002 |
| Předmět: |
Acrylamide
Binding Sites Cyclic gmp phosphodiesterase Transition (genetics) Protein Conformation Chemistry Circular Dichroism Temperature Phosphodiesterase chemistry.chemical_element Retinal General Chemistry Zinc Biochemistry Natively Unfolded Proteins chemistry.chemical_compound Spectrometry Fluorescence 3' 5'-Cyclic-GMP Phosphodiesterases Sequence Analysis Protein Signal transduction Protein Binding Gamma subunit |
| Zdroj: | Journal of Proteome Research. 1:149-159 |
| ISSN: | 1535-3907 1535-3893 |
| DOI: | 10.1021/pr0155127 |
| Popis: | 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. Keywords: cyclic GMP phosphodiesterase • signal transduction • intrinsically unordered protein • conformational transition • partially folded intermediate |
| Databáze: | OpenAIRE |
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