NMR assignments of the WBSCR27 protein related to Williams-Beuren syndrome

NMR assignments of the WBSCR27 protein related to Williams-Beuren syndrome Williams-Beuren syndrome is a genetic disorder characterized by physiological and mental abnormalities, and is caused by hemizygous deletion of several genes in chromosome 7. One of the removed genes encodes the WBSCR27 protein. Bioin- formatic analysis of the sequence of WBSCR27 indicates that it belongs to the family of SAM-dependent methyltransferases. However, exact cellular functions of this protein or phenotypic consequences of its deficiency are still unknown. Here we 1 15 13 report nearly complete H, N, and C chemical shifts assignments of the 26 kDa WBSCR27 protein from Mus musculus in complex with the cofactor S-adenosyl-l -methionine (SAM). Analysis of the assigned chemical shifts allowed us to charac- terize the protein’s secondary structure and backbone dynamics. The topology of the protein’s fold confirms the assumption that the WBSCR27 protein belongs to the family of class I methyltransferases. Keywords SAM-dependent methyltransferases · Williams-Beuren syndrome · Protein NMR · Resonance assignment · Secondary structure Abbreviations SAM S-Adenosyl-l -methionine TEV Tobacco Etch Virus nuclear-inclusion-a endopeptidase WBS Williams-Beuren syndrome * Chi-Fon Chang WBSCR W illiams-Beuren syndrome chromosome chifon@gate.sinica.edu.tw region * Vladimir I. Polshakov WBSCR27 Williams-Beuren Syndrome Chromosome vpolsha@mail.ru Region 27 protein Faculty of Fundamental Medicine, Center for Magnetic Tomography and Spectroscopy, M.V. Lomonosov Moscow State University, Moscow, Russia 119991 Biological context http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Biomolecular NMR Assignments Springer Journals
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Publisher
Springer Netherlands
Copyright
Copyright © 2018 by Springer Science+Business Media B.V., part of Springer Nature
Subject
Physics; Biological and Medical Physics, Biophysics; Polymer Sciences; Biochemistry, general
ISSN
1874-2718
eISSN
1874-270X
D.O.I.
10.1007/s12104-018-9827-2
Publisher site
See Article on Publisher Site

Abstract

Williams-Beuren syndrome is a genetic disorder characterized by physiological and mental abnormalities, and is caused by hemizygous deletion of several genes in chromosome 7. One of the removed genes encodes the WBSCR27 protein. Bioin- formatic analysis of the sequence of WBSCR27 indicates that it belongs to the family of SAM-dependent methyltransferases. However, exact cellular functions of this protein or phenotypic consequences of its deficiency are still unknown. Here we 1 15 13 report nearly complete H, N, and C chemical shifts assignments of the 26 kDa WBSCR27 protein from Mus musculus in complex with the cofactor S-adenosyl-l -methionine (SAM). Analysis of the assigned chemical shifts allowed us to charac- terize the protein’s secondary structure and backbone dynamics. The topology of the protein’s fold confirms the assumption that the WBSCR27 protein belongs to the family of class I methyltransferases. Keywords SAM-dependent methyltransferases · Williams-Beuren syndrome · Protein NMR · Resonance assignment · Secondary structure Abbreviations SAM S-Adenosyl-l -methionine TEV Tobacco Etch Virus nuclear-inclusion-a endopeptidase WBS Williams-Beuren syndrome * Chi-Fon Chang WBSCR W illiams-Beuren syndrome chromosome chifon@gate.sinica.edu.tw region * Vladimir I. Polshakov WBSCR27 Williams-Beuren Syndrome Chromosome vpolsha@mail.ru Region 27 protein Faculty of Fundamental Medicine, Center for Magnetic Tomography and Spectroscopy, M.V. Lomonosov Moscow State University, Moscow, Russia 119991 Biological context

Journal

Biomolecular NMR AssignmentsSpringer Journals

Published: Jun 4, 2018

References

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