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PDBsum entry 3l5i
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Immune system
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PDB id
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3l5i
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Contents |
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* Residue conservation analysis
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PDB id:
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Immune system
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Title:
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Crystal structure of fniii domains of human gp130 (domains 4-6)
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Structure:
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Interleukin-6 receptor subunit beta. Chain: a. Fragment: unp residues 323-612. Synonym: il-6r-beta, interleukin-6 signal transducer, membrane glycoprotein 130, gp130, cdw130, oncostatin-m receptor subunit alpha. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: gp130, il6st. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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1.90Å
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R-factor:
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0.184
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R-free:
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0.222
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Authors:
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N.J.Kershaw,J.-G.Zhang,T.P.J.Garrett,P.E.Czabotar
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Key ref:
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Y.Xu
et al.
(2010).
Crystal structure of the entire ectodomain of gp130: insights into the molecular assembly of the tall cytokine receptor complexes.
J Biol Chem,
285,
21214-21218.
PubMed id:
DOI:
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Date:
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22-Dec-09
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Release date:
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12-May-10
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PROCHECK
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Headers
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References
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P40189
(IL6RB_HUMAN) -
Interleukin-6 receptor subunit beta from Homo sapiens
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Seq:
Struc:
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918 a.a.
290 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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DOI no:
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J Biol Chem
285:21214-21218
(2010)
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PubMed id:
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Crystal structure of the entire ectodomain of gp130: insights into the molecular assembly of the tall cytokine receptor complexes.
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Y.Xu,
N.J.Kershaw,
C.S.Luo,
P.Soo,
M.J.Pocock,
P.E.Czabotar,
D.J.Hilton,
N.A.Nicola,
T.P.Garrett,
J.G.Zhang.
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ABSTRACT
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gp130 is the shared signal-transducing receptor subunit for the large and
important family of interleukin 6-like cytokines. Previous x-ray structures of
ligand-receptor complexes of this family lack the three membrane-proximal
domains that are essential for signal transduction. Here we report the crystal
structure of the entire extracellular portion of human gp130 (domains 1-6,
D1-D6) at 3.6 A resolution, in an unliganded form, as well as a higher
resolution structure of the membrane-proximal fibronectin type III domains
(D4-D6) at 1.9 A. This represents the first atomic resolution structure of the
complete ectodomain of any "tall" cytokine receptor. These structures show that
other than a reorientation of the D1 domain, there is little structural change
in gp130 upon ligand binding. They also reveal that the interface between the D4
and D5 domains forms an acute bend in the gp130 structure. Key residues at this
interface are highly conserved across the entire tall receptor family,
suggesting that this acute bend may be a common feature of these receptors.
Importantly, this geometry positions the C termini of the membrane-proximal
fibronectin type III domains of the tall cytokine receptors in close proximity
within the transmembrane complex, favorable for receptor-associated Janus
kinases to trans-phosphorylate and activate each other.
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Links
