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PDBsum entry 2n00
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DNA binding protein
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PDB id
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2n00
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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 nmr solution structure of aim2 pyd domain from mus musculus reveals a distinct α2-α3 helix conformation from its human homologues.
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Authors
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X.Hou,
X.Niu.
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Ref.
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Biochem Biophys Res Commun, 2015,
461,
396-400.
[DOI no: ]
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PubMed id
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Abstract
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The inflammasome is a key component of the innate immune system providing the
initial defense against invading organisms. Failure of inflammasome formation is
the main reason for many innate and acquired immune diseases. Cytosolic protein
absent in melanoma 2 (AIM2) has been reported to play an essential role in
double-stranded DNA (dsDNA) sensing and inflammasome formation in response to
viruses or bacteria infection. The N-terminal pyrin domain (PYD) of AIM2
interacts with the ASC PYD domain, and then recruits downstream proteins to
assemble the AIM2 inflammasome. The molecular mechanisms of PYD mediated
signaling remain elusive as limited structural information on PYD family.
Herein, we characterized the solution structure of mouse AIM2 PYD domain by NMR
spectroscopy, and compared it with the crystal structures of its two human
homologues. The comparison shows mAIM2 PYD adopts a unique α2-α3 helix
conformation distinct from its human homologues, but similar to the pyrin domain
of human NLRP10/PYNOD, which belongs to another family. In addition, the
aggregation of mAIM2 PYD domain, with the increased salt concentration, reveals
that both the charge surface and hydrophobic interaction play important roles in
the self-association of mAIM2 PYD.
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