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PDBsum entry 5zoj
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DNA binding protein
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PDB id
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5zoj
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Contents |
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187 a.a.
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127 a.a.
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116 a.a.
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References listed in PDB file
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Key reference
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Title
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Structural basis for receptor-Regulated smad recognition by man1.
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Authors
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K.I.Miyazono,
Y.Ohno,
H.Wada,
T.Ito,
Y.Fukatsu,
A.Kurisaki,
M.Asashima,
M.Tanokura.
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Ref.
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Nucleic Acids Res, 2018,
46,
12139-12153.
[DOI no: ]
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PubMed id
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Abstract
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Receptor-regulated SMAD (R-SMAD: SMAD1, SMAD2, SMAD3, SMAD5 and SMAD8) proteins
are key transcription factors of the transforming growth factor-β (TGF-β)
superfamily of cytokines. MAN1, an integral protein of the inner nuclear
membrane, is a SMAD cofactor that terminates TGF-β superfamily signals.
Heterozygous loss-of-function mutations in MAN1 result in osteopoikilosis,
Buschke-Ollendorff syndrome and melorheostosis. MAN1 interacts with MAD homology
2 (MH2) domains of R-SMAD proteins using its C-terminal U2AF homology motif
(UHM) domain and UHM ligand motif (ULM) and facilitates R-SMAD
dephosphorylation. Here, we report the structural basis for R-SMAD recognition
by MAN1. The SMAD2-MAN1 and SMAD1-MAN1 complex structures show that an
intramolecular UHM-ULM interaction of MAN1 forms a hydrophobic surface that
interacts with a hydrophobic surface among the H2 helix, the strands β8 and
β9, and the L3 loop of the MH2 domains of R-SMAD proteins. The complex
structures also show the mechanism by which SMAD cofactors distinguish R-SMAD
proteins that possess a highly conserved molecular surface.
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