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Angew Chem Int Ed Engl. 2014 Sep 8;53(37):9784-7. doi: 10.1002/anie.201404750. Epub 2014 Jul 1.

An unusual protein-protein interaction through coupled unfolding and binding.

Author information

1
Biomodulation Major, Department of Agricultural Biotechnology, Seoul National University, 1 Gwanak-ro, Gwanak-gu, Seoul 151-921 (South Korea).

Abstract

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.

KEYWORDS:

NMR spectroscopy; aptides; fibronectin; protein folding; protein-protein interactions

PMID:
24985319
DOI:
10.1002/anie.201404750
[Indexed for MEDLINE]
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