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PDBsum entry 2trc
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Complex (transducer/transduction)
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PDB id
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2trc
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Contents |
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340 a.a.
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68 a.a.
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217 a.a.
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure at 2.4 angstroms resolution of the complex of transducin betagamma and its regulator, Phosducin.
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Authors
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R.Gaudet,
A.Bohm,
P.B.Sigler.
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Ref.
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Cell, 1996,
87,
577-588.
[DOI no: ]
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PubMed id
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Abstract
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The crystal structure of transducin's betagamma subunits complexed with
phosducin, which regulates Gtbetagamma activity, has been solved to 2.4
angstroms resolution. Phosducin has two domains that wrap around Gtbetagamma to
form an extensive interface. The N-terminal domain binds loops on the "top"
Gtbeta surface, overlapping the Gtalpha binding surface, explaining how
phosducin blocks Gtbetagamma's interaction with Gtalpha. The C-terminal domain
shows structural homology to thioredoxin and binds the outer strands of Gtbeta's
seventh and first blades in a manner likely to disrupt Gtbetagamma's normal
orientation relative to the membrane and receptor. Phosducin's Ser-73, which
when phosphorylated inhibits phosducin's function, points away from Gtbetagamma,
toward a large flexible loop. Thus phosphorylation is not likely to affect the
interface directly, but rather indirectly through an induced conformational
change.
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Figure 4.
Figure 4. Structure of Phosducin(A) Stereo pair showing the
Cα trace of phosducin in the complex. The trace for residues 37
to 66 (open bars) is tentative. The N-terminal domain is at the
top and the C-terminal domain is at the bottom of the figure.
G[t]βγ would be located to the right of the N-terminal domain.
The Ser-73 α carbon is enlarged and labeled. This figure was
generated by DPLOT (G. Van Duyne).(B) Stereo pair showing the
least-squares superimposed Cα traces of the phosducin
C-terminal domain (blue) and thioredoxin ([18]) (red). The N-
and C-terminal residues of the C-terminal domain are labeled
P111 and P230, respectively. The N- and C-terminus of
thioredoxin are labeled T1 and T108. The C-terminal domain is
viewed from its left side, relative to (A), in an orientation
similar to that in Figure 6A.
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Figure 8.
Figure 8. Electrostatic Potential Representation of
Phosducin/G[t]βγ and G[t]βγ AloneElectrostatic potential
contoured at +1.5 kT (blue) and −1.5 kT (red) (ionic STRENGTH
= 100 mM). On the left is the phosducin/G[t]βγ complex, in the
same orientation as in Figure 6A. On the right is G[t]βγ
alone, in the same orientation. This figure was generated using
GRASP ([33]).
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The above figures are
reprinted
by permission from Cell Press:
Cell
(1996,
87,
577-588)
copyright 1996.
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Secondary reference #1
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Title
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Crystal structure of a g-Protein beta gamma dimer at 2.1a resolution.
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Authors
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J.Sondek,
A.Bohm,
D.G.Lambright,
H.E.Hamm,
P.B.Sigler.
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Ref.
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Nature, 1996,
379,
369-374.
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PubMed id
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