Methods for structure determination of SH2 domain-phosphopeptide complexes by NMR Journal Article
| Authors: | Nanna, V.; Marasco, M.; Kirkpatrick, J. P.; Carlomagno, T. |
| Article Title: | Methods for structure determination of SH2 domain-phosphopeptide complexes by NMR |
| 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. © 2023. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature. |
| Keywords: | nuclear magnetic resonance imaging; magnetic resonance imaging; magnetic resonance spectroscopy; nuclear magnetic resonance spectroscopy; structure determination; phosphotyrosine; intermolecular interactions; phosphopeptide; phosphopeptides; src homology domain; src homology domains; nuclear magnetic resonance (nmr) spectroscopy; src-homology 2 (sh2) domain |
| Journal Title: | Methods in Molecular Biology |
| Volume: | 2705 |
| ISSN: | 1064-3745 |
| Publisher: | Humana Press Inc |
| Date Published: | 2023-01-01 |
| Start Page: | 3 |
| End Page: | 23 |
| Language: | English |
| DOI: | 10.1007/978-1-0716-3393-9_1 |
| PUBMED: | 37668966 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Chapter 1 in "SH2 Domains: Functional Modules and Evolving Tools in Biology" (ISBN: 978-1-0716-3392-2) -- Source: Scopus |
