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PDBsum entry 4xhs
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Transport protein
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PDB id
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4xhs
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PDB id:
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| Name: |
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Transport protein
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Title:
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Crystal structure of human nlrp12 pyd domain and implication in homotypic interaction
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Structure:
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Maltose-binding periplasmic protein,nacht, lrr and pyd domains-containing protein 12. Chain: a, b. Fragment: unp p0aey0 residues 27-392, unp p59046 residues 10-106. Synonym: mbp,mmbp,maltodextrin-binding protein,monarch-1,pyrin- containing apaf1-like protein 7,regulated by nitric oxide. Engineered: yes
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Source:
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Escherichia coli o157:h7, homo sapiens. Human. Organism_taxid: 83334, 9606. Gene: male, z5632, ecs5017, nlrp12, nalp12, pypaf7, rno. Expressed in: escherichia coli. Expression_system_taxid: 511693.
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Resolution:
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1.70Å
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R-factor:
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0.161
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R-free:
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0.190
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Authors:
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T.Jin,M.Huang,J.Jiang,T.Xiao
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Key ref:
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T.Jin
et al.
(2018).
Crystal structure of human NLRP12 PYD domain and implication in homotypic interaction.
PLoS One,
13,
e0190547.
PubMed id:
DOI:
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Date:
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06-Jan-15
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Release date:
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27-Jan-16
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PROCHECK
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Headers
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References
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P0AEX9
(MALE_ECOLI) -
Maltose/maltodextrin-binding periplasmic protein from Escherichia coli (strain K12)
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Seq:
Struc:
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396 a.a.
452 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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*
PDB and UniProt seqs differ
at 13 residue positions (black
crosses)
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DOI no:
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PLoS One
13:e0190547
(2018)
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PubMed id:
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Crystal structure of human NLRP12 PYD domain and implication in homotypic interaction.
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T.Jin,
M.Huang,
J.Jiang,
P.Smith,
T.S.Xiao.
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ABSTRACT
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NLRP12 is a NOD-like receptor that plays multiple roles in both inflammation and
tumorigenesis. Despite the importance, little is known about its mechanism of
action at the molecular level. Here, we report the crystal structure of NLRP12
PYD domain at 1.70 Å fused with an maltose-binding protein (MBP) tag.
Interestingly, the PYD domain forms a dimeric configuration through a disulfide
bond in the crystal. The possible biological significance is discussed in the
context of ROS induced NF-κB activation.
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Links
