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PDBsum entry 2byf
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References listed in PDB file
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Key reference
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Title
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Structural and mechanistic insights into ras association domains of phospholipase c epsilon.
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Authors
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T.D.Bunney,
R.Harris,
N.L.Gandarillas,
M.B.Josephs,
S.M.Roe,
S.C.Sorli,
H.F.Paterson,
F.Rodrigues-Lima,
D.Esposito,
C.P.Ponting,
P.Gierschik,
L.H.Pearl,
P.C.Driscoll,
M.Katan.
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Ref.
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Mol Cell, 2006,
21,
495-507.
[DOI no: ]
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PubMed id
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Abstract
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Ras proteins signal to a number of distinct pathways by interacting with diverse
effectors. Studies of ras/effector interactions have focused on three classes,
Raf kinases, ral guanylnucleotide-exchange factors, and
phosphatidylinositol-3-kinases. Here we describe ras interactions with another
effector, the recently identified phospholipase C epsilon (PLCvarepsilon). We
solved structures of PLCvarepsilon RA domains (RA1 and RA2) by NMR and the
structure of the RA2/ras complex by X-ray crystallography. Although the
similarity between ubiquitin-like folds of RA1 and RA2 proves that they are
homologs, only RA2 can bind ras. Some of the features of the RA2/ras interface
are unique to PLCvarepsilon, while the ability to make contacts with both switch
I and II regions of ras is shared only with phosphatidylinositol-3-kinase.
Studies of PLCvarepsilon regulation suggest that, in a cellular context, the RA2
domain, in a mode specific to PLCvarepsilon, has a role in membrane targeting
with further regulatory impact on PLC activity.
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Figure 3.
Figure 3. Structural Perspectives of the Complex between
Ras and RA2
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Figure 6.
Figure 6. Model of Two-Step Mechanism of PLC  epsilon
Translocation and Activation
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The above figures are
reprinted
by permission from Cell Press:
Mol Cell
(2006,
21,
495-507)
copyright 2006.
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