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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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PDB id:
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| Name: |
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DNA binding protein
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Title:
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Crystal structure of human smad2-man1 complex
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Structure:
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Mothers against decapentaplegic homolog 2. Chain: a, b, c. Fragment: unp residues 262-458. Synonym: mothers against dpp homolog 2,jv18-1,mad-related protein 2, hmad-2,smad family member 2,hsmad2. Engineered: yes. Inner nuclear membrane protein man1. Chain: d, e. Fragment: unp residues 762-890.
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: smad2. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: man1. Expression_system_taxid: 562
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Resolution:
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2.79Å
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R-factor:
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0.243
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R-free:
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0.269
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Authors:
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K.Miyazono,Y.Ohno,T.Ito,M.Tanokura
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Key ref:
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K.I.Miyazono
et al.
(2018).
Structural basis for receptor-regulated SMAD recognition by MAN1.
Nucleic Acids Res,
46,
12139-12153.
PubMed id:
DOI:
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Date:
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13-Apr-18
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Release date:
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10-Oct-18
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PROCHECK
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Headers
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References
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Q15796
(SMAD2_HUMAN) -
Mothers against decapentaplegic homolog 2 from Homo sapiens
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Seq:
Struc:
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467 a.a.
187 a.a.
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Enzyme class:
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Chains A, B, C, D, E:
E.C.?
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DOI no:
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Nucleic Acids Res
46:12139-12153
(2018)
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PubMed id:
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Structural basis for receptor-regulated SMAD recognition by MAN1.
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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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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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Links
