Backbone resonance assignments for the SET domain of human methyltransferase NSD3 in complex with its cofactor

Backbone resonance assignments for the SET domain of human methyltransferase NSD3 in complex with its cofactor
Title:
Backbone resonance assignments for the SET domain of human methyltransferase NSD3 in complex with its cofactor
Other Titles:
Biomolecular NMR Assignments
DOI:
10.1007/s12104-017-9753-8
Publication Date:
14 August 2017
Citation:
Li, Y., Ng, H.Q., Ngo, A. et al. Biomol NMR Assign (2017) 11: 225. https://doi.org/10.1007/s12104-017-9753-8
Abstract:
NSD3 is a histone H3 methyltransferase that plays an important role in chromatin biology. A construct containing the methyltransferase domain encompassing residues Q1049-K1299 of human NSD3 was obtained and biochemical activity was demonstrated using histone as a substrate. Here we report the backbone HN, N, Ca, C’, and side chain Cβ assignments of the construct in complex with S-Adenosyl-L-methionine (SAM). Based on these assignments, secondary structure of NSD3/SAM complex in solution was determined.
License type:
PublisherCopyrights
Funding Info:
A*STAR JCO grant (1431AFG102/1331A028)
Description:
ISSN:
1874-2718
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