PDB ID or protein name

1a0r » Phosducin/Transducin beta-gamma complex, conformation 1

1a0r » Phosducin/Transducin beta-gamma complex, conformation 1
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Topology in Eukaryotic plasma membrane
Topologyextracellular side
cytoplasmic side
1a0r » Phosducin/Transducin beta-gamma complex, conformation 1
Depth 2.3 ± 1.0 Å
Tilt Angle 50 ± 4°
ΔGtransfer -7.4 kcal/mol
Links to 1a0r PDB Sum, PDB, SCOP, MSD, OCA, MMDB
Topology cytoplasmic
Resolution 2.8 Å
Other PDB entries representing this structure none
Number of subunits 3
2 references
Gaudet R, Savage JR, McLaughlin JN, Willardson BM, Sigler PB. 1999. A molecular mechanism for the phosphorylation-dependent regulation of heterotrimeric G proteins by phosducin. Mol Cell. 3:649-60. PubMed
Murray D, McLaughlin S, Honig B. 2001. The role of electrostatic interactions in the regulation of the membrane association of G protein beta gamma heterodimers. J Biol Chem. 276:45153-9. PubMed
Comments on 1a0r » Phosducin/Transducin beta-gamma complex, conformation 1
Phosducin probably facilitates removal of the beta-gamma complex from the membrane, starting from transfer of farnesyl from membrane to the binding cavity in beta-subunit (Gaudet et al. 1999). This is probably an initial membrane-bound state when phosducin is not phosphorylated. This orientation is similar to one proposed by Murray et al. (2001).