Tunable paramagnetic relaxation enhancements by [Gd(DPA)3] 3- for protein structure analysis

Hiromasa Yagi; Karin V. Loscha; Xun Cheng Su; Mitchell Stanton-Cook; Thomas Huber; Gottfried Otting

doi:10.1007/s10858-010-9416-x

Tunable paramagnetic relaxation enhancements by [Gd(DPA)₃] ^3- for protein structure analysis

Hiromasa Yagi, Karin V. Loscha, Xun Cheng Su, Mitchell Stanton-Cook, Thomas Huber, Gottfried Otting^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

22 Citations (Scopus)

Abstract

Paramagnetic relaxation enhancements (PRE) present a powerful source of structural information in nuclear magnetic resonance (NMR) studies of proteins and protein-ligand complexes. In contrast to conventional PRE reagents that are covalently attached to the protein, the complex between gadolinium and three dipicolinic acid (DPA) molecules, [Gd(DPA)₃]^3-, can bind to proteins in a non-covalent yet site-specific manner. This offers straightforward access to PREs that can be scaled by using different ratios of [Gd(DPA)₃]^3- to protein, allowing quantitative distance measurements for nuclear spins within about 15 Å of the Gd³⁺ ion. Such data accurately define the metal position relative to the protein, greatly enhancing the interpretation of pseudocontact shifts induced by [Ln(DPA)₃]^3- complexes of paramagnetic lanthanide (Ln ³⁺) ions other than gadolinium. As an example we studied the quaternary structure of the homodimeric GCN4 leucine zipper.

Original language	English
Pages (from-to)	143-153
Number of pages	11
Journal	Journal of Biomolecular NMR
Volume	47
Issue number	2
DOIs	https://doi.org/10.1007/s10858-010-9416-x
Publication status	Published - Jun 2010

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title = "Tunable paramagnetic relaxation enhancements by [Gd(DPA)3] 3- for protein structure analysis",

abstract = "Paramagnetic relaxation enhancements (PRE) present a powerful source of structural information in nuclear magnetic resonance (NMR) studies of proteins and protein-ligand complexes. In contrast to conventional PRE reagents that are covalently attached to the protein, the complex between gadolinium and three dipicolinic acid (DPA) molecules, [Gd(DPA)3]3-, can bind to proteins in a non-covalent yet site-specific manner. This offers straightforward access to PREs that can be scaled by using different ratios of [Gd(DPA)3]3- to protein, allowing quantitative distance measurements for nuclear spins within about 15 {\AA} of the Gd3+ ion. Such data accurately define the metal position relative to the protein, greatly enhancing the interpretation of pseudocontact shifts induced by [Ln(DPA)3]3- complexes of paramagnetic lanthanide (Ln 3+) ions other than gadolinium. As an example we studied the quaternary structure of the homodimeric GCN4 leucine zipper.",

keywords = "Lanthanide tags, Leucine zipper, NMR spectroscopy, Paramagnetic relaxation enhancements, Pseudocontact shifts",

author = "Hiromasa Yagi and Loscha, {Karin V.} and Su, {Xun Cheng} and Mitchell Stanton-Cook and Thomas Huber and Gottfried Otting",

year = "2010",

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doi = "10.1007/s10858-010-9416-x",

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AU - Loscha, Karin V.

AU - Su, Xun Cheng

AU - Stanton-Cook, Mitchell

AU - Huber, Thomas

AU - Otting, Gottfried

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Y1 - 2010/6

N2 - Paramagnetic relaxation enhancements (PRE) present a powerful source of structural information in nuclear magnetic resonance (NMR) studies of proteins and protein-ligand complexes. In contrast to conventional PRE reagents that are covalently attached to the protein, the complex between gadolinium and three dipicolinic acid (DPA) molecules, [Gd(DPA)3]3-, can bind to proteins in a non-covalent yet site-specific manner. This offers straightforward access to PREs that can be scaled by using different ratios of [Gd(DPA)3]3- to protein, allowing quantitative distance measurements for nuclear spins within about 15 Å of the Gd3+ ion. Such data accurately define the metal position relative to the protein, greatly enhancing the interpretation of pseudocontact shifts induced by [Ln(DPA)3]3- complexes of paramagnetic lanthanide (Ln 3+) ions other than gadolinium. As an example we studied the quaternary structure of the homodimeric GCN4 leucine zipper.

AB - Paramagnetic relaxation enhancements (PRE) present a powerful source of structural information in nuclear magnetic resonance (NMR) studies of proteins and protein-ligand complexes. In contrast to conventional PRE reagents that are covalently attached to the protein, the complex between gadolinium and three dipicolinic acid (DPA) molecules, [Gd(DPA)3]3-, can bind to proteins in a non-covalent yet site-specific manner. This offers straightforward access to PREs that can be scaled by using different ratios of [Gd(DPA)3]3- to protein, allowing quantitative distance measurements for nuclear spins within about 15 Å of the Gd3+ ion. Such data accurately define the metal position relative to the protein, greatly enhancing the interpretation of pseudocontact shifts induced by [Ln(DPA)3]3- complexes of paramagnetic lanthanide (Ln 3+) ions other than gadolinium. As an example we studied the quaternary structure of the homodimeric GCN4 leucine zipper.

KW - Lanthanide tags

KW - Leucine zipper

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KW - Pseudocontact shifts

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JO - Journal of Biomolecular NMR

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ER -

Tunable paramagnetic relaxation enhancements by [Gd(DPA)₃] ^3- for protein structure analysis

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