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

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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
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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