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PDBsum entry 6b5b
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Immune system
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PDB id
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6b5b
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Contents |
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1199 a.a.
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903 a.a.
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68 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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The structural basis of flagellin detection by naip5: a strategy to limit pathogen immune evasion.
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Authors
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J.L.Tenthorey,
N.Haloupek,
J.R.López-Blanco,
P.Grob,
E.Adamson,
E.Hartenian,
N.A.Lind,
N.M.Bourgeois,
P.Chacón,
E.Nogales,
R.E.Vance.
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Ref.
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Science, 2017,
358,
888-893.
[DOI no: ]
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PubMed id
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Abstract
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Robust innate immune detection of rapidly evolving pathogens is critical for
host defense. Nucleotide-binding domain leucine-rich repeat (NLR) proteins
function as cytosolic innate immune sensors in plants and animals. However, the
structural basis for ligand-induced NLR activation has so far remained unknown.
NAIP5 (NLR family, apoptosis inhibitory protein 5) binds the bacterial protein
flagellin and assembles with NLRC4 to form a multiprotein complex called an
inflammasome. Here we report the cryo-electron microscopy structure of the
assembled ~1.4-megadalton flagellin-NAIP5-NLRC4 inflammasome, revealing how a
ligand activates an NLR. Six distinct NAIP5 domains contact multiple conserved
regions of flagellin, prying NAIP5 into an open and active conformation. We show
that innate immune recognition of multiple ligand surfaces is a generalizable
strategy that limits pathogen evolution and immune escape.
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