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PDBsum entry 3dm0
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Sugar binding protein,signaling protein
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PDB id
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3dm0
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References listed in PDB file
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Key reference
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Title
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Structure of a signal transduction regulator, Rack1, From arabidopsis thaliana.
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Authors
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H.Ullah,
E.L.Scappini,
A.F.Moon,
L.V.Williams,
D.L.Armstrong,
L.C.Pedersen.
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Ref.
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Protein Sci, 2008,
17,
1771-1780.
[DOI no: ]
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PubMed id
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Abstract
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The receptor for activated C-kinase 1 (RACK1) is a highly conserved WD40 repeat
scaffold protein found in a wide range of eukaryotic species from Chlamydymonas
to plants and humans. In tissues of higher mammals, RACK1 is ubiquitously
expressed and has been implicated in diverse signaling pathways involving
neuropathology, cellular stress, protein translation, and developmental
processes. RACK1 has established itself as a scaffold protein through physical
interaction with a myriad of signaling proteins ranging from kinases,
phosphatases, ion channels, membrane receptors, G proteins, IP3 receptor, and
with widely conserved structural proteins associated with the ribosome. In the
plant Arabidopsis thaliana, RACK1A is implicated in diverse developmental and
environmental stress pathways. Despite the functional conservation of
RACK1-mediated protein-protein interaction-regulated signaling modes, the
structural basis of such interactions is largely unknown. Here we present the
first crystal structure of a RACK1 protein, RACK1 isoform A from Arabidopsis
thaliana, at 2.4 A resolution, as a C-terminal fusion of the maltose binding
protein. The structure implicates highly conserved surface residues that could
play critical roles in protein-protein interactions and reveals the surface
location of proposed post-transcriptionally modified residues. The availability
of this structure provides a structural basis for dissecting RACK1-mediated
cellular signaling mechanisms in both plants and animals.
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Figure 2.
Figure 2. Ribbon diagram of Asp–His–Ser
hydrogen-bonding network responsible for maintaining the
integrity of the β-sheet within blade 2 of the β-propeller.
His62 lies on the loop connecting blade 1 with blade 2. Trp90
and Asp91 represent the WD repeat of blade 2.
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Figure 4.
Figure 4. Surface diagrams of conserved regions within the
RACK1 proteins. (A) Conserved region 1. Conserved residues are
colored according to the blade to which they belong based on the
ribbon diagram in Figure 1B. Residues Arg36, Trp83, Arg125,
Trp152, and Lys214 line the upper rim of the β-propeller pore.
(B) Conserved region 2. Tyr230 and Tyr248 on RACK1A are proposed
phosphorylation sites. Residue Pro204 is located on the lower
rim of the pore of the β-propeller. Molecular surfaces were
created using PyMOL (DeLano Scientific).
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The above figures are
reprinted
by permission from the Protein Society:
Protein Sci
(2008,
17,
1771-1780)
copyright 2008.
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