NMR Methods to Study the Dynamics of SH2 Domain-Phosphopeptide Complexes.

Michelangelo Marasco; John Kirkpatrick; Vittoria Nanna; Teresa Carlomagno

doi:10.1007/978-1-0716-3393-9_2

NMR Methods to Study the Dynamics of SH2 Domain-Phosphopeptide Complexes.

Michelangelo Marasco, John Kirkpatrick, Vittoria Nanna, Teresa Carlomagno^*

^*Corresponding author for this work

Biosciences

Research output: Chapter in Book/Report/Conference proceeding › Chapter (peer-reviewed) › peer-review

Abstract

Nuclear magnetic resonance (NMR) spectroscopy is the method of choice for studying the dynamics of biological macromolecules in solution. By exploiting the intricate interplay between the effects of protein motion (both overall rotational diffusion and internal mobility) and nuclear spin relaxation, NMR allows molecular motion to be probed at atomic resolution over a wide range of timescales, including picosecond (bond vibrations and methyl-group rotations), nanosecond (loop motions and rotational diffusion), and microsecond–millisecond (ligand binding, allostery). In this chapter, we describe different NMR pulse schemes (R1, R1ρ, heteronuclear NOE, and CPMG relaxation dispersion) to characterize the dynamics of SH2 domains. As an example, we use the N-SH2 domain of protein tyrosine phosphatase SHP2 in complex with two phosphopeptides derived from immune checkpoint receptor PD-1 (ITIM and ITSM).

Original language	English
Title of host publication	SH2 Domains
Subtitle of host publication	Functional Modules and Evolving Tools in Biology
Editors	Teresa Carlomagno, Maja Köhn
Publisher	Humana Press
Pages	25-37
Number of pages	12
Edition	1
ISBN (Electronic)	9781071633939
ISBN (Print)	9781071633922, 9781071633953
DOIs	https://doi.org/10.1007/978-1-0716-3393-9_2
Publication status	Published - 6 Sept 2023

Publication series

Name	Methods in molecular biology
Publisher	Springer
Volume	2705
ISSN (Print)	1064-3745
ISSN (Electronic)	1940-6029

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title = "NMR Methods to Study the Dynamics of SH2 Domain-Phosphopeptide Complexes.",

abstract = "Nuclear magnetic resonance (NMR) spectroscopy is the method of choice for studying the dynamics of biological macromolecules in solution. By exploiting the intricate interplay between the effects of protein motion (both overall rotational diffusion and internal mobility) and nuclear spin relaxation, NMR allows molecular motion to be probed at atomic resolution over a wide range of timescales, including picosecond (bond vibrations and methyl-group rotations), nanosecond (loop motions and rotational diffusion), and microsecond–millisecond (ligand binding, allostery). In this chapter, we describe different NMR pulse schemes (R1, R1ρ, heteronuclear NOE, and CPMG relaxation dispersion) to characterize the dynamics of SH2 domains. As an example, we use the N-SH2 domain of protein tyrosine phosphatase SHP2 in complex with two phosphopeptides derived from immune checkpoint receptor PD-1 (ITIM and ITSM).",

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NMR Methods to Study the Dynamics of SH2 Domain-Phosphopeptide Complexes. / Marasco, Michelangelo; Kirkpatrick, John; Nanna, Vittoria et al.
SH2 Domains: Functional Modules and Evolving Tools in Biology. ed. / Teresa Carlomagno; Maja Köhn. 1. ed. Humana Press, 2023. p. 25-37 (Methods in molecular biology; Vol. 2705).

Research output: Chapter in Book/Report/Conference proceeding › Chapter (peer-reviewed) › peer-review

TY - CHAP

T1 - NMR Methods to Study the Dynamics of SH2 Domain-Phosphopeptide Complexes.

AU - Marasco, Michelangelo

AU - Kirkpatrick, John

AU - Nanna, Vittoria

AU - Carlomagno, Teresa

PY - 2023/9/6

Y1 - 2023/9/6

N2 - Nuclear magnetic resonance (NMR) spectroscopy is the method of choice for studying the dynamics of biological macromolecules in solution. By exploiting the intricate interplay between the effects of protein motion (both overall rotational diffusion and internal mobility) and nuclear spin relaxation, NMR allows molecular motion to be probed at atomic resolution over a wide range of timescales, including picosecond (bond vibrations and methyl-group rotations), nanosecond (loop motions and rotational diffusion), and microsecond–millisecond (ligand binding, allostery). In this chapter, we describe different NMR pulse schemes (R1, R1ρ, heteronuclear NOE, and CPMG relaxation dispersion) to characterize the dynamics of SH2 domains. As an example, we use the N-SH2 domain of protein tyrosine phosphatase SHP2 in complex with two phosphopeptides derived from immune checkpoint receptor PD-1 (ITIM and ITSM).

AB - Nuclear magnetic resonance (NMR) spectroscopy is the method of choice for studying the dynamics of biological macromolecules in solution. By exploiting the intricate interplay between the effects of protein motion (both overall rotational diffusion and internal mobility) and nuclear spin relaxation, NMR allows molecular motion to be probed at atomic resolution over a wide range of timescales, including picosecond (bond vibrations and methyl-group rotations), nanosecond (loop motions and rotational diffusion), and microsecond–millisecond (ligand binding, allostery). In this chapter, we describe different NMR pulse schemes (R1, R1ρ, heteronuclear NOE, and CPMG relaxation dispersion) to characterize the dynamics of SH2 domains. As an example, we use the N-SH2 domain of protein tyrosine phosphatase SHP2 in complex with two phosphopeptides derived from immune checkpoint receptor PD-1 (ITIM and ITSM).

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DO - 10.1007/978-1-0716-3393-9_2

M3 - Chapter (peer-reviewed)

SN - 9781071633922

SN - 9781071633953

T3 - Methods in molecular biology

SP - 25

EP - 37

BT - SH2 Domains

A2 - Carlomagno, Teresa

A2 - Köhn, Maja

PB - Humana Press

ER -

NMR Methods to Study the Dynamics of SH2 Domain-Phosphopeptide Complexes.

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