| Autor: |
Uversky VN; Institute for Biological Instrumentation, Russian Academy of Sciences, 142290 Pushchino, Russia. uversky@hydrogen.ucsc.edu, Permyakov SE, Zagranichny VE, Rodionov IL, Fink AL, Cherskaya AM, Wasserman LA, Permyakov EA |
| Jazyk: |
angličtina |
| Zdroj: |
Journal of proteome research [J Proteome Res] 2002 Mar-Apr; Vol. 1 (2), pp. 149-59. |
| DOI: |
10.1021/pr0155127 |
| Abstrakt: |
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. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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