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PDBsum entry 1na0
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De novo protein
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PDB id
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1na0
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Contents |
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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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Design of stable alpha-Helical arrays from an idealized tpr motif.
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Authors
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E.R.Main,
Y.Xiong,
M.J.Cocco,
L.D'Andrea,
L.Regan.
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Ref.
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Structure, 2003,
11,
497-508.
[DOI no: ]
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PubMed id
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Abstract
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The tetratricopeptide repeat (TPR) is a 34-amino acid alpha-helical motif that
occurs in over 300 different proteins. In the different proteins, three to
sixteen or more TPR motifs occur in tandem arrays and function to mediate
protein-protein interactions. The binding specificity of each TPR protein is
different, although the underlying structural motif is the same. Here we
describe a statistical approach to the design of an idealized TPR motif. We
present the high-resolution X-ray crystal structures (to 1.55 and 1.6 A) of
designed TPR proteins and describe their solution properties and stability. A
detailed analysis of these structures provides an understanding of the TPR
motif, how it is repeated to give helical arrays with different superhelical
twists, and how a very stable framework may be constructed for future functional
designs.
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Figure 3.
Figure 3. Structural Features of CTPR2/3(A) Representation
of the electron density of CTPR2 in the vicinity of Tyr23(B2)
and Tyr24(B2). A 2F[o] - F[c] map (blue), contoured at 1 s, is
displayed over a stick model of the structure to demonstrate the
quality of the data.(B-D) Representation of the overall folds of
(B) CTPR2 and (C) CTPR3 and (D) a stereo view of the overlaid
structures of CTPR2 (red) and CTPR3 (blue). They are represented
by a tubular worm that snakes through their C^a backbones. CTPR2
(red) corresponds to 86 amino acids from Gly3 to Gly15(solvating
helix), and CTPR3 (blue) corresponds to 119 amino acids from
Asn2 to Gly15(solvating helix). The N and C termini are marked
on each diagram.(E) An illustration showing the two IPTG
molecules (space fill, purple and blue) that induce a dimer
interface between two molecules of CTPR3 (rendered as a cyan and
red C^a trace). The side chains of residues that interact with
the IPTG are rendered as sticks, with the chloride ion caught
between the two IPTG molecules rendered as green space fills.
(A)-(E) were produced with SPOCK [53].
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2003,
11,
497-508)
copyright 2003.
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