An Unusual protein-protein interaction through coupled unfolding and binding

Tae Kyung Yu, Seung A. Shin, Eun Hee Kim, Sunghyun Kim, Kyung Seok Ryu, Haekap Cheong, Hee Chul Ahn, Sangyong Jon, Jeong Yong Suh

Research output: Contribution to journalArticlepeer-review

11 Scopus citations

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.

Original languageEnglish
Pages (from-to)9784-9787
Number of pages4
JournalAngewandte Chemie - International Edition
Volume53
Issue number37
DOIs
StatePublished - 8 Sep 2014

Keywords

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

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