title: Effect of zinc and temperature on the conformation of the gamma subunit of retinal phosphodiesterase: a natively unfolded protein.
abstract: 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.
authors.affiliation: Institute for Biological Instrumentation, Russian Academy of Sciences, 142290 Pushchino, Russia. uversky@hydrogen.ucsc.edu
authors.forename: Vladimir N
authors.initials: VN
authors.lastname: Uversky
authors.forename: Sergey E
authors.initials: SE
authors.lastname: Permyakov
authors.forename: Vasily E
authors.initials: VE
authors.lastname: Zagranichny
authors.forename: Igor L
authors.initials: IL
authors.lastname: Rodionov
authors.forename: Anthony L
authors.initials: AL
authors.lastname: Fink
authors.forename: Alexandra M
authors.initials: AM
authors.lastname: Cherskaya
authors.forename: Lyubov A
authors.initials: LA
authors.lastname: Wasserman
authors.forename: Eugene A
authors.initials: EA
authors.lastname: Permyakov
mesh_terms: D015106:3',5'-Cyclic-GMP Phosphodiesterases / Q000737:chemistry / Q000378:metabolism*; D020106:Acrylamide / Q000737:chemistry; D001665:Binding Sites; D002942:Circular Dichroism; D011485:Protein Binding; D011487:Protein Conformation; D020539:Sequence Analysis, Protein; D013050:Spectrometry, Fluorescence; D013696:Temperature; D015032:Zinc / Q000378:metabolism*
chemical_list: D020106:Acrylamide; D015106:3',5'-Cyclic-GMP Phosphodiesterases; D015032:Zinc