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PDBsum entry 4l59
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Transcription
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PDB id
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4l59
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References listed in PDB file
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Key reference
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Title
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The structure-Activity relationships of l3mbtl3 inhibitors: flexibility of the dimer interface.
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Authors
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M.A.Camerino,
N.Zhong,
A.Dong,
B.M.Dickson,
L.I.James,
B.M.Baughman,
J.L.Norris,
D.B.Kireev,
W.P.Janzen,
C.H.Arrowsmith,
S.V.Frye.
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Ref.
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Medchemcomm, 2013,
4,
1501-1507.
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PubMed id
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Abstract
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We recently reported the discovery of UNC1215, a potent and selective chemical
probe for the L3MBTL3 methyllysine reader domain. In this article, we describe
the development of structure-activity relationships (SAR) of a second series of
potent L3MBTL3 antagonists which evolved from the structure of the chemical
probe UNC1215. These compounds are selective for L3MBTL3 against a panel of
methyllysine reader proteins, particularly the related MBT family proteins,
L3MBTL1 and MBTD1. A co-crystal structure of L3MBTL3 and one of the most potent
compounds suggests that the L3MBTL3 dimer rotates about the dimer interface to
accommodate ligand binding.
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