Protein-protein interaction that involves coupled unfolding and binding

by 관리자 posted Nov 20, 2014
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초청강사 서 정 용 교수
소속 서울대학교 농생명공학부
일시 2014.11.13(목) 오후 5시
장소 아산이학관 331호

Aptides is a novel class of high-affinity peptides that recognize diverse molecular targets with high affinity and specificity. Here we report the solution structure of an aptide APT specifically bound to fibronectin extradomain B (EDB), a prominent marker of tumor angiogenesis. The complex structure reveals an unusual protein-protein interaction via coupled unfolding and binding. APT binding is accompanied by unfolding of the C-terminal β strand of EDB, permitting APT to interact with fresh-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. Unfolding of EDB perturbs the tight domain association between EDB and FN8 of fibronectin, highlighting its potential use as a scaffold that switches between stretched and bent conformations.