PDBsum entry 3l5h

Immune system

PDB id: 3l5h

Contents

Protein chain

585 a.a. *

Ligands

NAG-NAG ×3

NAG-NAG-BMA-BMA ×2

NAG-NAG-BMA

NAG-FUC

SO4 ×3

* Residue conservation analysis

PDB id:

3l5h

Name:

Immune system

Title:

Crystal structure of the full ectodomain of human gp130: new insights into the molecular assembly of receptor complexes

Structure:

Interleukin-6 receptor subunit beta. Chain: a. Fragment: ecotodomain. Synonym: il-6r-beta, interleukin-6 signal transducer, membrane glycoprotein 130, gp130, cdw130, oncostatin-m receptor subunit alpha. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: il6st. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Expression_system_cell_line: sf21.

Resolution:

3.60Å R-factor: 0.267 R-free: 0.335

Authors:

Y.Xu,T.P.J.Garrett,J.G.Zhang

Key ref:

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: 20489211 DOI: 10.1074/jbc.C110.129502

Date:

21-Dec-09 Release date: 19-May-10

Protein chain

P40189  (IL6RB_HUMAN) -  Interleukin-6 receptor subunit beta from Homo sapiens

Seq: 918 a.a.

Struc: 585 a.a.

DOI no: 10.1074/jbc.C110.129502

J Biol Chem 285:21214-21218 (2010)

PubMed id: 20489211

Crystal structure of the entire ectodomain of gp130: insights into the molecular assembly of the tall cytokine receptor complexes.

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.

ABSTRACT

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.