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PDBsum entry 2mnu
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Cell adhesion
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PDB id
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2mnu
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References listed in PDB file
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Key reference
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Title
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An unusual protein-Protein interaction through coupled unfolding and binding.
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Authors
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T.K.Yu,
S.A.Shin,
E.H.Kim,
S.Kim,
K.S.Ryu,
H.Cheong,
H.C.Ahn,
S.Jon,
J.Y.Suh.
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Ref.
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Angew Chem Int Ed Engl, 2014,
53,
9784-9787.
[DOI no: ]
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PubMed id
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Abstract
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Aptides, a novel class of high-affinity peptides, recognize diverse molecular
targets with high affinity and specificity. The solution structure of the aptide
APT specifically bound to fibronectin extradomain B (EDB), which represents an
unusual protein-protein interaction that involves coupled unfolding and binding,
is reported. APT binding is accompanied by unfolding of the C-terminal
β strand of EDB, thereby permitting APT to interact with the freshly exposed
hydrophobic interior surfaces of EDB. The β-hairpin scaffold of APT drives the
interaction by a β-strand displacement mechanism, such that an intramolecular
β sheet is replaced by an intermolecular β sheet. The unfolding of EDB
perturbs the tight domain association between EDB and FN8 of fibronectin, thus
highlighting its potential use as a scaffold that switches between stretched and
bent conformations.
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