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Methods for Structure Determination of SH2 Domain-Phosphopeptide Complexes by NMR.
Nanna, Vittoria; Marasco, Michelangelo; Kirkpatrick, John P; Carlomagno, Teresa.
Afiliação
  • Nanna V; BMWZ and Institute of Organic Chemistry, Leibniz University Hannover, Hannover, Germany.
  • Marasco M; School of Biosciences, University of Birmingham, Birmingham, UK.
  • Kirkpatrick JP; Molecular Pharmacology Program, Sloan Kettering Institute for Cancer Research, Memorial Sloan Kettering Cancer Center, New York, NY, USA.
  • Carlomagno T; School of Biosciences, University of Birmingham, Birmingham, UK.
Methods Mol Biol ; 2705: 3-23, 2023.
Article em En | MEDLINE | ID: mdl-37668966
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.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Fosfopeptídeos / Domínios de Homologia de src Idioma: En Revista: Methods Mol Biol Ano de publicação: 2023 Tipo de documento: Article

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Fosfopeptídeos / Domínios de Homologia de src Idioma: En Revista: Methods Mol Biol Ano de publicação: 2023 Tipo de documento: Article