The same pocket in menin binds both MLL and JUND but has opposite effects on transcription

Jing Huang, Buddha Gurung, Bingbing Wan, Smita Matkar, Natalia A. Veniaminova, Ke Wan, Juanita L. Merchant, Xianxin Hua () and Ming Lei ()
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Jing Huang: Howard Hughes Medical Institute, University of Michigan Medical School, 1150 West. Medical Center Drive
Buddha Gurung: Abramson Family Cancer Research Institute, University of Pennsylvania Perelman School of Medicine
Bingbing Wan: Howard Hughes Medical Institute, University of Michigan Medical School, 1150 West. Medical Center Drive
Smita Matkar: Abramson Family Cancer Research Institute, University of Pennsylvania Perelman School of Medicine
Natalia A. Veniaminova: University of Michigan, 109 Zina Pitcher Place, Ann Arbor, Michigan 48109, USA
Ke Wan: Howard Hughes Medical Institute, University of Michigan Medical School, 1150 West. Medical Center Drive
Juanita L. Merchant: University of Michigan, 109 Zina Pitcher Place, Ann Arbor, Michigan 48109, USA
Xianxin Hua: Abramson Family Cancer Research Institute, University of Pennsylvania Perelman School of Medicine
Ming Lei: Howard Hughes Medical Institute, University of Michigan Medical School, 1150 West. Medical Center Drive

Nature, 2012, vol. 482, issue 7386, 542-546

Abstract: Crystal structures of menin in its free form and in complexes with MLL1 or with JUND, or with an MLL1–LEDGF heterodimer, show that menin contains a deep pocket that binds short peptides of MLL1 or JUND in the same manner, but produces opposite effects on transcription.

Date: 2012
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DOI: 10.1038/nature10806

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