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 ( K d ∼1 μM), with His75 and His79 being directly involved into the coordination of Zn 2+ . Zinc-loaded protein remains effectively unfolded. Possible implications of these findings to the functioning of PDEγ are discussed.
No takes yet. Share an insight, caveat, or question.
Uversky et al. (2002) studied this question.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: