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TitleStructural Studies Provide New Insights into the Role of Lysine Acetylation on Substrate Recognition by CARM1 and Inform the Design of Potent Peptidomimetic Inhibitors.
Journal, issue, pagesChembiochem, Vol. 22, Page 3469-3476, Year 2021
Publish dateMay 18, 2021 (structure data deposition date)
AuthorsZhang, Y. / Marechal, N. / van Haren, M.J. / Troffer-Charlier, N. / Cura, V. / Cavarelli, J. / Martin, N.I.
External linksChembiochem / PubMed:34569136
MethodsX-ray diffraction
Resolution2.2 - 2.54 Å
Structure data

PDB-7okp:
Crystal structure of mouse CARM1 in complex with histone H3_13-22 K18 acetylated
Method: X-RAY DIFFRACTION / Resolution: 2.2 Å

PDB-7os4:
Crystal structure of mouse CARM1 in complex with histone H3_13-31 K18
Method: X-RAY DIFFRACTION / Resolution: 2.54 Å

Chemicals

ChemComp-MLI:
MALONATE ION

ChemComp-QVR:
(2~{R},3~{R},4~{S},5~{R})-2-(6-aminopurin-9-yl)-5-[(~{E})-prop-1-enyl]oxolane-3,4-diol

ChemComp-HOH:
WATER

Source
  • mus musculus (house mouse)
  • homo sapiens (human)
KeywordsTRANSCRIPTION / protein arginine N-methyltransferase / PRMT / CARM1 / transition state mimics

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