Issue 40, 2010
From the journal:

Chemical Communications

Two-dimensional heteronuclear saturation transfer difference NMR reveals detailed integrin αvβ6protein–peptide interactions†

Jane L. Wagstaff,a   Sabari Vallath,b   John F. Marshall,b   Richard A. Williamson*a  and  Mark J. Howard*a  

* Corresponding authors

a Protein Science Group, School of Biosciences, University of Kent, Canterbury, Kent, UK
E-mail: m.j.howard@kent.ac.uk, r.a.williamson@kent.ac.uk
Fax: +44 (0)1227 763912
Tel: +44 (0)1227 764000

b Queen Mary University of London, Barts and The London School of Medicine and Dentistry, Institute of Cancer and CRUK Clinical Centre, John Vane Science Centre, Charterhouse Square, London, UK
E-mail: j.f.marshall@qmul.ac.uk
Fax: +44 (0)207 882 3884
Tel: +44 (0)207 882 3580

Abstract

We report the first example of peptide–protein heteronuclear two-dimensional (2D) saturation transfer difference nuclear magnetic resonance (STD NMR). This method, resulting in dramatically reduced overlap, was applied to the interaction of the integrin αvβ6 with a known peptide ligand and highlights novel contact points between the substrate and target protein.

Graphical abstract: Two-dimensional heteronuclear saturation transfer difference NMR reveals detailed integrin αvβ6 protein–peptide interactions

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Article information

DOI
https://doi.org/10.1039/C0CC01846E
Article type
Communication
Submitted
11 Jun 2010
Accepted
24 Aug 2010
First published
13 Sep 2010

Chem. Commun., 2010,46, 7533-7535

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Two-dimensional heteronuclear saturation transfer difference NMR reveals detailed integrin αvβ6 protein–peptide interactions

J. L. Wagstaff, S. Vallath, J. F. Marshall, R. A. Williamson and M. J. Howard, Chem. Commun., 2010, 46, 7533 DOI: 10.1039/C0CC01846E

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