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

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Biomolecular NMR Assignments : Volume 10, Issue 1, April 2016

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Biomolecular NMR Assignments : Volume 1

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

Content Provider	Springer Nature Link
Author	Amin, Nader Nietlispach, Daniel Qamar, Seema Coyle, Joe Chiarparin, Elisabetta Williams, Glyn
Copyright Year	2016
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.
Starting Page	315
Ending Page	320
Page Count	6
File Format	PDF
ISSN	18742718
Journal	Biomolecular NMR Assignments
Volume Number	10
Issue Number	2
e-ISSN	1874270X
Language	English
Publisher	Springer Netherlands
Publisher Date	2016-06-29
Publisher Place	Dordrecht
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Nuclear receptor-binding SET domain NSD1 NSD2 MMSET WHSC1 NSD family Histone-methyl transferase NMR resonance assignments NMR stability screen Biophysics and Biological Physics Polymer Sciences Biochemistry
Content Type	Text
Resource Type	Article
Subject	Structural Biology Biochemistry

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Backbone resonance assignments for the SET domain of the human methyltransferase NSD2

In vitro histone lysine methylation by NSD1, NSD2/MMSET/WHSC1 and NSD3/WHSC1L

In vitro histone lysine methylation by NSD1, NSD2/MMSET/WHSC1 and NSD3/WHSC1L

The Methyltransferase NSD3 Has Chromatin-binding Motifs, PHD5-C5HCH, That Are Distinct from Other NSD (Nuclear Receptor SET Domain) Family Members in Their Histone H3 Recognition

Backbone assignment of the little finger domain of a Y-family DNA polymerase

Backbone resonance assignment of the BCL6-BTB/POZ domain

$^{1}$H, $^{13}$C, $^{15}$N backbone and side-chain resonance assignments of the Bright/ARID domain from the human histone demethylase JARID1B

Small Molecule Inhibitors of the Human Histone Lysine Methyltransferase NSD2 / WHSC1 / MMSET Identified from a Quantitative High-Throughput Screen with Nucleosome Substrate

Backbone and sidechain $^{1}$H, $^{13}$C and $^{15}$N resonance assignments of the Bright/ARID domain from the human JARID1C (SMCX) protein

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

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