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

Sofia S. Mariasina, Olga A. Petrova, Ilya A. Osterman, Olga V. Sergeeva, Sergey V. Efimov, Vladimir V. Klochkov, Petr V. Sergiev, Olga A. Dontsova, Tai huang Huang, Chi Fon Chang, Vladimir I. Polshakov*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

3 Citations (Scopus)


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. Bioinformatic 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 report nearly complete 1H, 15N, and 13C 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 characterize 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.

Original languageEnglish
Pages (from-to)303-308
Number of pages6
JournalBiomolecular NMR Assignments
Issue number2
Publication statusPublished - 2018 Oct 1


  • Protein NMR
  • Resonance assignment
  • SAM-dependent methyltransferases
  • Secondary structure
  • Williams-Beuren syndrome

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry


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