Methods for Structure Determination of SH2 Domain-Phosphopeptide Complexes by NMR

Vittoria Nanna; Michelangelo Marasco; John P Kirkpatrick; Teresa Carlomagno

doi:10.1007/978-1-0716-3393-9_1

Methods for Structure Determination of SH2 Domain-Phosphopeptide Complexes by NMR

Methods Mol Biol. 2023:2705:3-23. doi: 10.1007/978-1-0716-3393-9_1.

Authors

Vittoria Nanna^{1

2}, Michelangelo Marasco³, John P Kirkpatrick², Teresa Carlomagno⁴

Affiliations

¹ BMWZ and Institute of Organic Chemistry, Leibniz University Hannover, Hannover, Germany.
² School of Biosciences, University of Birmingham, Birmingham, UK.
³ Molecular Pharmacology Program, Sloan Kettering Institute for Cancer Research, Memorial Sloan Kettering Cancer Center, New York, NY, USA.
⁴ School of Biosciences, College of Life and Environmental Sciences, University of Birmingham, Birmingham, UK. t.carlomagno@bham.ac.uk.

PMID: 37668966
DOI: 10.1007/978-1-0716-3393-9_1

Abstract

Nuclear magnetic resonance (NMR) spectroscopy is a powerful technique to solve the structure of biomolecular complexes at atomic resolution in solution. Small proteins such as Src-homology 2 (SH2) domains have fast tumbling rates and long-lived NMR signals, making them particularly suited to be studied by standard NMR methods. SH2 domains are modular proteins whose function is the recognition of sequences containing phosphotyrosines. In this chapter, we describe the application of NMR to assess the interaction between SH2 domains and phosphopeptides and determine the structure of the resulting complexes.

Keywords: Intermolecular interactions; Nuclear magnetic resonance (NMR) spectroscopy; Phosphopeptides; Phosphotyrosine; Src-homology 2 (SH2) domain; Structure determination.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Magnetic Resonance Imaging
Magnetic Resonance Spectroscopy
Phosphopeptides*
Phosphotyrosine
src Homology Domains*

Substances

Phosphopeptides
Phosphotyrosine