The chemical shift assignment of gamma subunit of phosphodiesterase

Proceedings of the National Academy of Sciences of the United States of America
Intrinsically disordered gamma-subunit of cGMP phosphodiesterase encodes functionally relevant transient secondary and tertiary structure.

cGMP-phosphodiesterase gamma subunit [Canis lupus familiaris]

cGMP phosphodiesterase gamma subunit [Felis catus]

cGMP phosphodiesterase gamma inhibitory subunit [synthetic construct]

cyclic-GMP phosphodiesterase gamma subunit [Canis lupus familiaris]

rCG33796, isoform CRA_b [Rattus norvegicus]

retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma [Canis lupus familiaris]

retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma [Bos taurus]

PREDICTED: retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma [Rattus norvegicus]

PREDICTED: retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma [Equus caballus]

RecName: Full=Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma; Short=GMP-PDE gamma

The deposited chemical shifts were assigned only for the protein A68-PDEgamma,
in which no paramagnetic relaxation enhancement probe was added. The structures
deposited in PDB (2ju4) were calculated using the combined distance restraints
derived from ten single PDEgamma mutants (on each mutant a native residue was
replaced by the 3-maleimido-PROXYL-cysteine residue). As a result, the PDB
structures contain 10 mutated residues which do not coexist in the process of
NMR structure determination.

Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax