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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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PDB id:
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| Name: |
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Transcription
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Title:
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Crystal structure of the 3-mbt repeat domain of l3mbtl3 and unc2533 complex
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Structure:
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Lethal(3)malignant brain tumor-like protein 3. Chain: a. Synonym: h-l(3)mbt-like protein 3, l(3)mbt-like protein 3, mbt-1. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: l3mbtl3, kiaa1798, mbt1. Expressed in: escherichia coli. Expression_system_taxid: 511693.
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Resolution:
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2.29Å
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R-factor:
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0.213
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R-free:
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0.250
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Authors:
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N.Zhong,A.Dong,M.Ravichandran,M.A.Camerino,B.M.Dickson,L.I.James, B.M.Baughman,J.L.Norris,D.B.Kireev,W.P.Janzen,S.Graslund,S.V.Frye, C.Bountra,A.M.Edwards,C.H.Arrowsmith,P.J.Brown,Structural Genomics Consortium (Sgc)
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Key ref:
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M.A.Camerino
et al.
(2013).
The structure-activity relationships of L3MBTL3 inhibitors: flexibility of the dimer interface.
Medchemcomm,
4,
1501-1507.
PubMed id:
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Date:
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10-Jun-13
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Release date:
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10-Jul-13
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PROCHECK
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Headers
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References
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Q96JM7
(LMBL3_HUMAN) -
Lethal(3)malignant brain tumor-like protein 3 from Homo sapiens
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Seq:
Struc:
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780 a.a.
307 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Medchemcomm
4:1501-1507
(2013)
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PubMed id:
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The structure-activity relationships of L3MBTL3 inhibitors: flexibility of the dimer interface.
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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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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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