PDBsum entry 2mnu

Cell adhesion

PDB id: 2mnu

Contents

Protein chains

93 a.a.

26 a.a.

PDB id:

2mnu

Name:

Cell adhesion

Title:

Backbone and side chain 1h, 13c, and 15n chemical shift assignments for edb and specific binding aptide

Structure:

Edb. Chain: a. Engineered: yes. Apt. Chain: b. Engineered: yes

Source:

Homo sapiens. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.

NMR struc:

20 models

Authors:

J.Suh,T.Yu

Key ref:

T.K.Yu et al. (2014). An unusual protein-protein interaction through coupled unfolding and binding. Angew Chem Int Ed Engl, 53, 9784-9787. PubMed id: 24985319 DOI: 10.1002/anie.201404750

Date:

10-Apr-14 Release date: 24-Sep-14

Protein chain

P02751  (FINC_HUMAN) -  Fibronectin from Homo sapiens

Seq: 2477 a.a.

Struc: 93 a.a.*

Protein chain

No UniProt id for this chain

Struc: 26 a.a.

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

DOI no: 10.1002/anie.201404750

Angew Chem Int Ed Engl 53:9784-9787 (2014)

PubMed id: 24985319

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

T.K.Yu, S.A.Shin, E.H.Kim, S.Kim, K.S.Ryu, H.Cheong, H.C.Ahn, S.Jon, J.Y.Suh.

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.