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PDBsum entry 3lqm
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Protein binding
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PDB id
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3lqm
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Contents |
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* Residue conservation analysis
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PDB id:
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Protein binding
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Title:
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Structure of the il-10r2 common chain
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Structure:
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Interleukin-10 receptor subunit beta. Chain: a, b. Fragment: extracellular domain. Synonym: il-10 receptor subunit beta, il-10r subunit beta, il-10rb, interleukin-10 receptor subunit 2, il-10r subunit 2, il-10r2, cytokine receptor family 2 member 4, crf2-4, cytokine receptor class- ii member 4. Engineered: yes. Mutation: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108
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Resolution:
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2.14Å
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R-factor:
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0.210
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R-free:
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0.239
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Authors:
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S.I.Yoon,M.R.Walter
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Key ref:
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S.I.Yoon
et al.
(2010).
Structure and mechanism of receptor sharing by the IL-10R2 common chain.
Structure,
18,
638-648.
PubMed id:
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Date:
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09-Feb-10
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Release date:
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26-May-10
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PROCHECK
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Headers
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References
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Q08334
(I10R2_HUMAN) -
Interleukin-10 receptor subunit beta from Homo sapiens
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Seq:
Struc:
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325 a.a.
201 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 6 residue positions (black
crosses)
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Structure
18:638-648
(2010)
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PubMed id:
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Structure and mechanism of receptor sharing by the IL-10R2 common chain.
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S.I.Yoon,
B.C.Jones,
N.J.Logsdon,
B.D.Harris,
A.Deshpande,
S.Radaeva,
B.A.Halloran,
B.Gao,
M.R.Walter.
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ABSTRACT
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IL-10R2 is a shared cell surface receptor required for the activation of five
class 2 cytokines (IL-10, IL-22, IL-26, IL-28, and IL-29) that play critical
roles in host defense. To define the molecular mechanisms that regulate its
promiscuous binding, we have determined the crystal structure of the IL-10R2
ectodomain at 2.14 A resolution. IL-10R2 residues required for binding were
identified by alanine scanning and used to derive computational models of
IL-10/IL-10R1/IL-10R2 and IL-22/IL-22R1/IL-10R2 ternary complexes. The models
reveal a conserved binding epitope that is surrounded by two clefts that
accommodate the structural and chemical diversity of the cytokines. These
results provide a structural framework for interpreting IL-10R2 single
nucleotide polymorphisms associated with human disease.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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L.Prokunina-Olsson,
B.Muchmore,
W.Tang,
R.M.Pfeiffer,
H.Park,
H.Dickensheets,
D.Hergott,
P.Porter-Gill,
A.Mumy,
I.Kohaar,
S.Chen,
N.Brand,
M.Tarway,
L.Liu,
F.Sheikh,
J.Astemborski,
H.L.Bonkovsky,
B.R.Edlin,
C.D.Howell,
T.R.Morgan,
D.L.Thomas,
B.Rehermann,
R.P.Donnelly,
and
T.R.O'Brien
(2013).
A variant upstream of IFNL3 (IL28B) creating a new interferon gene IFNL4 is associated with impaired clearance of hepatitis C virus.
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Nat Genet,
45,
164-171.
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W.Ouyang,
S.Rutz,
N.K.Crellin,
P.A.Valdez,
and
S.G.Hymowitz
(2011).
Regulation and functions of the IL-10 family of cytokines in inflammation and disease.
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Annu Rev Immunol,
29,
71.
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A.P.Hinck
(2010).
Class II cytokine common receptors: something old, something new.
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Structure,
18,
551-552.
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R.P.Donnelly,
F.Sheikh,
H.Dickensheets,
R.Savan,
H.A.Young,
and
M.R.Walter
(2010).
Interleukin-26: an IL-10-related cytokine produced by Th17 cells.
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Cytokine Growth Factor Rev,
21,
393-401.
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R.Sabat,
G.Grütz,
K.Warszawska,
S.Kirsch,
E.Witte,
K.Wolk,
and
J.Geginat
(2010).
Biology of interleukin-10.
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Cytokine Growth Factor Rev,
21,
331-344.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
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