2MNU

Backbone and side chain 1H, 13C, and 15N Chemical Shift Assignments for EDB and specific binding aptide

Summary for 2MNU

• Entry DOI: 10.2210/pdb2mnu/pdb
• NMR Information: BMRB: 19906
• Descriptor: EDB, APT (2 entities in total)
• Functional Keywords: edb, aptide, cell adhesion
• Biological source: Homo sapiens; More
• Total number of polymer chains: 2
• Total formula weight: 12938.25

Authors

Suh, J.,Yu, T. (deposition date: 2014-04-10, release date: 2014-09-24, Last modification date: 2024-05-15)

Primary citation

Yu, T.K.,Shin, S.A.,Kim, E.H.,Kim, S.,Ryu, K.S.,Cheong, H.,Ahn, H.C.,Jon, S.,Suh, J.Y.
An Unusual Protein-Protein Interaction through Coupled Unfolding and Binding
Angew.Chem.Int.Ed.Engl., 53:9784-9787, 2014

PubMed 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.

PubMed: 24985319
DOI: 10.1002/anie.201404750

Experimental method

SOLUTION NMR