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Structure paper

TitleThe same pocket in menin binds both MLL and JUND but has opposite effects on transcription.
Journal, issue, pagesNature, Vol. 482, Page 542-546, Year 2012
Publish dateOct 15, 2011 (structure data deposition date)
AuthorsHuang, J. / Gurung, B. / Wan, B. / Matkar, S. / Veniaminova, N.A. / Wan, K. / Merchant, J.L. / Hua, X. / Lei, M.
External linksNature / PubMed:22327296
MethodsX-ray diffraction
Resolution2.5 - 3 Å
Structure data

PDB-3u84:
Crystal Structure of Human Menin
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-3u85:
Crystal structure of human menin in complex with MLL1
Method: X-RAY DIFFRACTION / Resolution: 3 Å

PDB-3u86:
Crystal structure of human menin in complex with JunD
Method: X-RAY DIFFRACTION / Resolution: 2.843 Å

PDB-3u88:
Crystal structure of human menin in complex with MLL1 and LEDGF
Method: X-RAY DIFFRACTION / Resolution: 3 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-CHD:
CHOLIC ACID

ChemComp-GGB:
L-CANAVANINE

ChemComp-0BR:
(4beta,8alpha,9R)-6'-methoxy-10,11-dihydrocinchonan-9-ol

ChemComp-GLV:
GLYOXYLIC ACID

ChemComp-SO4:
SULFATE ION

Source
  • homo sapiens (human)
KeywordsTRANSCRIPTION / menin / MEN1 / MLL / JunD / LEDGF / TPR / transglutaminase-like / epigenetics / cancer

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