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PDBsum entry 1a17
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References listed in PDB file
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Key reference
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Title
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The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for tpr-Mediated protein-Protein interactions.
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Authors
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A.K.Das,
P.W.Cohen,
D.Barford.
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Ref.
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EMBO J, 1998,
17,
1192-1199.
[DOI no: ]
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PubMed id
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Abstract
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The tetratricopeptide repeat (TPR) is a degenerate 34 amino acid sequence
identified in a wide variety of proteins, present in tandem arrays of 3-16
motifs, which form scaffolds to mediate protein-protein interactions and often
the assembly of multiprotein complexes. TPR-containing proteins include the
anaphase promoting complex (APC) subunits cdc16, cdc23 and cdc27, the NADPH
oxidase subunit p67 phox, hsp90-binding immunophilins, transcription factors,
the PKR protein kinase inhibitor, and peroxisomal and mitochondrial import
proteins. Here, we report the crystal structure of the TPR domain of a protein
phosphatase, PP5. Each of the three TPR motifs of this domain consist of a pair
of antiparallel alpha-helices of equivalent length. Adjacent TPR motifs are
packed together in a parallel arrangement such that a tandem TPR motif structure
is composed of a regular series of antiparallel alpha-helices. The uniform
angular and spatial arrangement of neighbouring alpha-helices defines a helical
structure and creates an amphipathic groove. Multiple-TPR motif proteins would
fold into a right-handed super-helical structure with a continuous helical
groove suitable for the recognition of target proteins, hence defining a novel
mechanism for protein recognition. The spatial arrangement of alpha-helices in
the PP5-TPR domain is similar to those within 14-3-3 proteins.
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Figure 1.
Figure 1 Schematic of TPR-containing proteins. TPR motifs (shown
as boxes) are observed as multiple tandem repeats and also
separated by sequence insertions.
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Figure 2.
Figure 2 Stereo view of the electron density map of the PP5 -TPR
domain calculated to 2.5 Å resolution using experimental phases
with the refined coordinates superimposed. The figure was
produced using O (Jones et al., 1991).
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The above figures are
reprinted
from an Open Access publication published by Macmillan Publishers Ltd:
EMBO J
(1998,
17,
1192-1199)
copyright 1998.
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