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Biomolecular NMR Assignments

, Volume 10, Issue 2, pp 315–320 | Cite as

NMR backbone resonance assignment and solution secondary structure determination of human NSD1 and NSD2

  • Nader Amin
  • Daniel Nietlispach
  • Seema Qamar
  • Joe Coyle
  • Elisabetta Chiarparin
  • Glyn WilliamsEmail author
Article

Abstract

Proteins of the NSD family are histone-methyl transferases with critical functions in the regulation of chromatin structure and function. NSD1 and NSD2 are homologous proteins that function as epigenetic regulators of transcription through their abilities to catalyse histone methylation. Misregulation of NSD1 and NSD2 expression or mutations in their genes are linked to a number of human diseases such as Sotos syndrome, and cancers including acute myeloid leukemia, multiple myeloma, and lung cancer. The catalytic domain of both proteins contains a conserved SET domain which is involved in histone methylation. Here we report the backbone resonance assignments and secondary structure information of the catalytic domains of human NSD1 and NSD2.

Keywords

Nuclear receptor-binding SET domain NSD1 NSD2 MMSET WHSC1 NSD family Histone-methyl transferase NMR resonance assignments NMR stability screen 

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Copyright information

© Springer Science+Business Media Dordrecht 2016

Authors and Affiliations

  • Nader Amin
    • 1
    • 4
  • Daniel Nietlispach
    • 2
  • Seema Qamar
    • 3
  • Joe Coyle
    • 1
  • Elisabetta Chiarparin
    • 1
    • 5
  • Glyn Williams
    • 1
    Email author
  1. 1.Astex PharmaceuticalsCambridgeUK
  2. 2.Department of BiochemistryUniversity of CambridgeCambridgeUK
  3. 3.Cambridge Institute for Medical ResearchUniversity of CambridgeCambridgeUK
  4. 4.Nuffield Department of Population HealthUniversity of OxfordOxfordUK
  5. 5.AstraZenecaCambridgeUK

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