title: NMR backbone resonance assignment and solution secondary structure determination of human NSD1 and NSD2.
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.
authors.affiliation: Astex Pharmaceuticals, 436 Cambridge Science Park, Cambridge, CB4 0QA, UK.|Nuffield Department of Population Health, University of Oxford, Richard Doll Building, Oxford, OX3 7LF, UK.
authors.forename: Nader
authors.initials: N
authors.lastname: Amin
authors.affiliation: Department of Biochemistry, University of Cambridge, 80 Tennis Court Rd, Cambridge, CB2 1GA, UK.
authors.forename: Daniel
authors.initials: D
authors.lastname: Nietlispach
authors.affiliation: Cambridge Institute for Medical Research, University of Cambridge, Hills Road, Cambridge, CB2 0XY, UK.
authors.forename: Seema
authors.initials: S
authors.lastname: Qamar
authors.affiliation: Astex Pharmaceuticals, 436 Cambridge Science Park, Cambridge, CB4 0QA, UK.
authors.forename: Joe
authors.initials: J
authors.lastname: Coyle
authors.affiliation: Astex Pharmaceuticals, 436 Cambridge Science Park, Cambridge, CB4 0QA, UK.|AstraZeneca, 310 Cambridge Science Park, Cambridge, CB4 0WG, UK.
authors.forename: Elisabetta
authors.initials: E
authors.lastname: Chiarparin
authors.affiliation: Astex Pharmaceuticals, 436 Cambridge Science Park, Cambridge, CB4 0QA, UK. glyn.williams@astx.com.
authors.forename: Glyn
authors.initials: G
authors.lastname: Williams
mesh_terms: D000595:Amino Acid Sequence; D000076983:Histone Methyltransferases; D011495:Histone-Lysine N-Methyltransferase / Q000737:chemistry*; D006801:Humans; D047908:Intracellular Signaling Peptides and Proteins / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D009687:Nuclear Proteins / Q000737:chemistry*; D000072417:Protein Domains; D017433:Protein Structure, Secondary; D012097:Repressor Proteins / Q000737:chemistry*; D012996:Solutions
chemical_list: D047908:Intracellular Signaling Peptides and Proteins; D009687:Nuclear Proteins; D012097:Repressor Proteins; D012996:Solutions; D000076983:Histone Methyltransferases; D011495:Histone-Lysine N-Methyltransferase; C113272:NSD1 protein, human; C419586:NSD2 protein, human
keywords: Histone-methyl transferase; MMSET; NMR resonance assignments; NMR stability screen; NSD family; NSD1; NSD2; Nuclear receptor-binding SET domain; WHSC1