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PDBsum entry 4v3o
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De novo protein
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PDB id
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4v3o
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References listed in PDB file
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Key reference
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Title
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Structures of designed armadillo-Repeat proteins show propagation of inter-Repeat interface effects.
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Authors
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C.Reichen,
C.Madhurantakam,
S.Hansen,
M.G.Grütter,
A.Plückthun,
P.R.Mittl.
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Ref.
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Acta Crystallogr D Struct Biol, 2016,
72,
168-175.
[DOI no: ]
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PubMed id
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Abstract
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The armadillo repeat serves as a scaffold for the development of modular
peptide-recognition modules. In order to develop such a system, three crystal
structures of designed armadillo-repeat proteins with third-generation N-caps
(YIII-type), four or five internal repeats (M-type) and second-generation C-caps
(AII-type) were determined at 1.8 Å (His-YIIIM4AII), 2.0 Å (His-YIIIM5AII)
and 1.95 Å (YIIIM5AII) resolution and compared with those of variants with
third-generation C-caps. All constructs are full consensus designs in which the
internal repeats have exactly the same sequence, and hence identical
conformations of the internal repeats are expected. The N-cap and internal
repeats M1 to M3 are indeed extremely similar, but the comparison reveals
structural differences in internal repeats M4 and M5 and the C-cap. These
differences are caused by long-range effects of the C-cap, contacting molecules
in the crystal, and the intrinsic design of the repeat. Unfortunately, the
rigid-body movement of the C-terminal part impairs the regular arrangement of
internal repeats that forms the putative peptide-binding site. The
second-generation C-cap improves the packing of buried residues and thereby the
stability of the protein. These considerations are useful for future
improvements of an armadillo-repeat-based peptide-recognition system.
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