 |
PDBsum entry 3jbl
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
|
|
|
|
|
|
|
Immune system
|
PDB id
|
|
|
|
3jbl
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
PDB id:
|
 |
|
 |
| Name: |
 |
Immune system
|
 |
|
Title:
|
 |
Cryo-em structure of the activated naip2/nlrc4 inflammasome reveals nucleated polymerization
|
|
Structure:
|
 |
Nlr family card domain-containing protein 4. Chain: k, a, b, c, d, e, f, g, h, i, j. Fragment: unp residues 93-1024, see remark 999. Synonym: nlrc4, caspase recruitment domain-containing protein 12, ice protease-activating factor, ipaf. Engineered: yes
|
|
Source:
|
 |
Mus musculus. Mouse. Organism_taxid: 10090. Strain: raw 264.7. Cell_line: macrophage. Tissue: abelson murine leukemia virus-induced tumor. Ascites. Cellular_location: cytosol. Gene: nlrc4, card12, ipaf. Expressed in: spodoptera frugiperda.
|
|
Authors:
|
 |
L.Zhang,S.Chen,J.Ruan,J.Wu,A.B.Tong,Q.Yin,Y.Li,L.David,A.Lu,W.L.Wang, C.Marks,Q.Ouyang,X.Zhang,Y.Mao,H.Wu
|
|
Key ref:
|
 |
L.Zhang
et al.
(2015).
Cryo-EM structure of the activated NAIP2-NLRC4 inflammasome reveals nucleated polymerization.
Science,
350,
404-409.
PubMed id:
DOI:
|
 |
|
Date:
|
 |
|
05-Sep-15
|
Release date:
|
21-Oct-15
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
Headers
|
 |
|
|
References
|
|
|
|
|
|
|
Q3UP24
(NLRC4_MOUSE) -
NLR family CARD domain-containing protein 4 from Mus musculus
|
|
|
|
Seq: Struc:
|
 |
 |
 |
1024 a.a.
909 a.a.
|
|
|
|
|
|
|
|
|
 |
 |
|
|
|
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
| |
|
DOI no:
|
Science
350:404-409
(2015)
|
|
PubMed id:
|
|
|
|
|
| |
|
Cryo-EM structure of the activated NAIP2-NLRC4 inflammasome reveals nucleated polymerization.
|
|
L.Zhang,
S.Chen,
J.Ruan,
J.Wu,
A.B.Tong,
Q.Yin,
Y.Li,
L.David,
A.Lu,
W.L.Wang,
C.Marks,
Q.Ouyang,
X.Zhang,
Y.Mao,
H.Wu.
|
|
|
|
| |
ABSTRACT
|
|
|
| |
|
The NLR family apoptosis inhibitory proteins (NAIPs) bind conserved bacterial
ligands, such as the bacterial rod protein PrgJ, and recruit NLR family
CARD-containing protein 4 (NLRC4) as the inflammasome adapter to activate innate
immunity. We found that the PrgJ-NAIP2-NLRC4 inflammasome is assembled into
multisubunit disk-like structures through a unidirectional adenosine
triphosphatase polymerization, primed with a single PrgJ-activated NAIP2 per
disk. Cryo-electron microscopy (cryo-EM) reconstruction at subnanometer
resolution revealed a ~90° hinge rotation accompanying NLRC4 activation. Unlike
in the related heptameric Apaf-1 apoptosome, in which each subunit needs to be
conformationally activated by its ligand before assembly, a single
PrgJ-activated NAIP2 initiates NLRC4 polymerization in a domino-like reaction to
promote the disk assembly. These insights reveal the mechanism of signal
amplification in NAIP-NLRC4 inflammasomes.
|
|
|
|
|
|
|
 |
 |
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
');
}
}
 |