Assignment of the orphan nuclear receptor Nurr1 by NMR

Paul Michiels; Karen Atkins; Christian Ludwig; Sara Whittaker; Maria Van Dongen; Ulrich Günther

doi:10.1007/s12104-010-9210-4

Assignment of the orphan nuclear receptor Nurr1 by NMR

Paul Michiels, Karen Atkins, Christian Ludwig, Sara Whittaker, Maria Van Dongen, Ulrich Günther^*

^*Corresponding author for this work

Institute of Chemistry and Metabolomics

University of Birmingham

9 Citations (Scopus)

Abstract

The orphan nuclear receptor Nurr1 has been implicated in a number of conditions including Parkinson's disease and Schizophrenia. As such, it is of interest to study its interactions with other proteins, possibly mediated by small molecules, considering possible use as a drug target. We produced ²H, ¹⁵N, ¹³C labelled-Nurr1 to generate the backbone amide NH, carbonyl C′, C_alpha and C_beta assignments. About 84.0% of residues could be assigned. Most of the 37 missing assignments fall in 3 regions of the protein. Two of these surround a putative ligand-binding region of Nurr1, suggesting that this region of the protein is flexible, despite the ligand-binding pocket being filled with hydrophobic side-chains from residues surrounding the ligand binding pocket.

Original language	English
Journal	Biomolecular NMR Assignments
Volume	4
Issue number	1
Pages (from-to)	101-105
Number of pages	5
ISSN	1874-2718
DOIs	https://doi.org/10.1007/s12104-010-9210-4
Publication status	Published - 04.2010

Research Areas and Centers

Academic Focus: Center for Infection and Inflammation Research (ZIEL)

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

Access to Document

10.1007/s12104-010-9210-4

Cite this

@article{1aa5576c79fc4ad481c385b7b50b6572,

title = "Assignment of the orphan nuclear receptor Nurr1 by NMR",

abstract = "The orphan nuclear receptor Nurr1 has been implicated in a number of conditions including Parkinson's disease and Schizophrenia. As such, it is of interest to study its interactions with other proteins, possibly mediated by small molecules, considering possible use as a drug target. We produced 2H, 15N, 13C labelled-Nurr1 to generate the backbone amide NH, carbonyl C′, Calpha and Cbeta assignments. About 84.0\% of residues could be assigned. Most of the 37 missing assignments fall in 3 regions of the protein. Two of these surround a putative ligand-binding region of Nurr1, suggesting that this region of the protein is flexible, despite the ligand-binding pocket being filled with hydrophobic side-chains from residues surrounding the ligand binding pocket.",

author = "Paul Michiels and Karen Atkins and Christian Ludwig and Sara Whittaker and \{Van Dongen\}, Maria and Ulrich G{\"u}nther",

year = "2010",

month = apr,

doi = "10.1007/s12104-010-9210-4",

language = "English",

volume = "4",

pages = "101--105",

journal = "Biomolecular NMR Assignments",

issn = "1874-2718",

number = "1",

}

TY - JOUR

T1 - Assignment of the orphan nuclear receptor Nurr1 by NMR

AU - Michiels, Paul

AU - Atkins, Karen

AU - Ludwig, Christian

AU - Whittaker, Sara

AU - Van Dongen, Maria

AU - Günther, Ulrich

PY - 2010/4

Y1 - 2010/4

N2 - The orphan nuclear receptor Nurr1 has been implicated in a number of conditions including Parkinson's disease and Schizophrenia. As such, it is of interest to study its interactions with other proteins, possibly mediated by small molecules, considering possible use as a drug target. We produced 2H, 15N, 13C labelled-Nurr1 to generate the backbone amide NH, carbonyl C′, Calpha and Cbeta assignments. About 84.0% of residues could be assigned. Most of the 37 missing assignments fall in 3 regions of the protein. Two of these surround a putative ligand-binding region of Nurr1, suggesting that this region of the protein is flexible, despite the ligand-binding pocket being filled with hydrophobic side-chains from residues surrounding the ligand binding pocket.

AB - The orphan nuclear receptor Nurr1 has been implicated in a number of conditions including Parkinson's disease and Schizophrenia. As such, it is of interest to study its interactions with other proteins, possibly mediated by small molecules, considering possible use as a drug target. We produced 2H, 15N, 13C labelled-Nurr1 to generate the backbone amide NH, carbonyl C′, Calpha and Cbeta assignments. About 84.0% of residues could be assigned. Most of the 37 missing assignments fall in 3 regions of the protein. Two of these surround a putative ligand-binding region of Nurr1, suggesting that this region of the protein is flexible, despite the ligand-binding pocket being filled with hydrophobic side-chains from residues surrounding the ligand binding pocket.

UR - https://www.scopus.com/pages/publications/77951808899

U2 - 10.1007/s12104-010-9210-4

DO - 10.1007/s12104-010-9210-4

M3 - Journal articles

C2 - 20300892

AN - SCOPUS:77951808899

SN - 1874-2718

VL - 4

SP - 101

EP - 105

JO - Biomolecular NMR Assignments

JF - Biomolecular NMR Assignments

IS - 1

ER -

Assignment of the orphan nuclear receptor Nurr1 by NMR

Abstract

Research Areas and Centers

UN SDGs

Access to Document

Other files and links

Fingerprint

Cite this