2mnu

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

spinqualitylabelsall models 2mnu, 20 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2mnu is a 2 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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 beta strand of EDB, thereby permitting APT to interact with the freshly exposed hydrophobic interior surfaces of EDB. The beta-hairpin scaffold of APT drives the interaction by a beta-strand displacement mechanism, such that an intramolecular beta sheet is replaced by an intermolecular beta 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. An Unusual Protein-Protein Interaction through Coupled Unfolding and Binding.,Yu TK, Shin SA, Kim EH, Kim S, Ryu KS, Cheong H, Ahn HC, Jon S, Suh JY Angew Chem Int Ed Engl. 2014 Sep 8;53(37):9784-7. doi: 10.1002/anie.201404750., Epub 2014 Jul 1. PMID:24985319 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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