 |
PDBsum entry 3wo3
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Immune system
|
PDB id
|
|
|
|
3wo3
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
(+ 0 more)
156 a.a.
|
|
|
|
|
|
|
|
|
|
|
294 a.a.
|
|
|
|
|
|
|
|
|
|
|
272 a.a.
|
|
|
|
|
|
|
|
|
|
|
255 a.a.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
PDB id:
|
|
|
|
| Name: |
|
Immune system
|
|
|
Title:
|
|
Crystal structure of il-18 in complex with il-18 receptor alpha
|
|
Structure:
|
|
Interleukin-18. Chain: a, c, e, g, i, k. Synonym: il-18, iboctadekin, interferon gamma-inducing factor, ifn- gamma-inducing factor, interleukin-1 gamma, il-1 gamma. Engineered: yes. Interleukin-18 receptor 1. Chain: b, d, f, h, j, l. Fragment: unp residues 20-329. Synonym: interleukin-18 receptor alpha, il-18r-1, il-18r1, cd218
|
|
Source:
|
|
Homo sapiens. Human. Organism_taxid: 9606. Gene: il18. Expressed in: escherichia coli. Expression_system_taxid: 562. Gene: il18r1. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108.
|
|
Resolution:
|
|
|
3.10Å
|
R-factor:
|
0.192
|
R-free:
|
0.222
|
|
|
Authors:
|
|
N.Tsutsumi,T.Kimura,K.Arita,M.Ariyoshi,H.Ohnishi,N.Kondo,M.Shirakawa, Z.Kato,H.Tochio
|
|
Key ref:
|
|
N.Tsutsumi
et al.
(2014).
The structural basis for receptor recognition of human interleukin-18.
Nat Commun,
5,
5340.
PubMed id:
DOI:
|
|
|
Date:
|
|
|
19-Dec-13
|
Release date:
|
17-Dec-14
|
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
|
Headers
|
|
|
|
References
|
|
|
|
|
|
|
|
Q14116
(IL18_HUMAN) -
Interleukin-18 from Homo sapiens
|
|
|
|
Seq:
Struc:
|
|
|
|
193 a.a.
156 a.a.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Q13478
(IL18R_HUMAN) -
Interleukin-18 receptor 1 from Homo sapiens
|
|
|
|
Seq:
Struc:
|
|
|
|
541 a.a.
294 a.a.*
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Enzyme class:
|
|
Chains B, D, F, H, J, L:
E.C.3.2.2.6
- ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase.
|
|
|
|
|
|
|
Reaction:
|
|
NAD+ + H2O = ADP-D-ribose + nicotinamide + H+
|
|
|
|
|
|
NAD(+)
|
+
|
H2O
|
=
|
ADP-D-ribose
|
+
|
nicotinamide
|
+
|
H(+)
Bound ligand (Het Group name = )
matches with 43.75% similarity
|
|
|
|
|
|
|
|
|
|
|
|
|
Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
|
| |
|
DOI no:
|
Nat Commun
5:5340
(2014)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
The structural basis for receptor recognition of human interleukin-18.
|
|
N.Tsutsumi,
T.Kimura,
K.Arita,
M.Ariyoshi,
H.Ohnishi,
T.Yamamoto,
X.Zuo,
K.Maenaka,
E.Y.Park,
N.Kondo,
M.Shirakawa,
H.Tochio,
Z.Kato.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
Interleukin (IL)-18 is a proinflammatory cytokine that belongs to the IL-1
family and plays an important role in inflammation. The uncontrolled release of
this cytokine is associated with severe chronic inflammatory disease. IL-18
forms a signalling complex with the IL-18 receptor α (Rα) and β (Rβ) chains
at the plasma membrane, which induces multiple inflammatory cytokines. Here, we
present a crystal structure of human IL-18 bound to the two receptor
extracellular domains. Generally, the receptors' recognition mode for IL-18 is
similar to IL-1β; however, certain notable differences were observed. The
architecture of the IL-18 receptor second domain (D2) is unique among the other
IL-1R family members, which presumably distinguishes them from the IL-1
receptors that exhibit a more promiscuous ligand recognition mode. The
structures and associated biochemical and cellular data should aid in developing
novel drugs to neutralize IL-18 activity.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
| | |
Links
