PDBsum entry 1bqu

Signaling protein

PDB id: 1bqu

Contents

Protein chains

208 a.a. *

Ligands

SO4 ×6

GOL ×5

Waters ×277

* Residue conservation analysis

PDB id:

1bqu

Name:

Signaling protein

Title:

Cytokyne-binding region of gp130

Structure:

Protein (gp130). Chain: a, b. Fragment: cytokine-binding region domains. Engineered: yes. Other_details: interleukin-6 receptor beta fragment interleukin 6 signal transducer membrane glycoprotein 130 gp130 oncostatin m receptor

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: il6st. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.00Å R-factor: 0.221 R-free: 0.255

Authors:

J.Bravo,D.Staunton,J.K.Heath,E.Y.Jones

Key ref:

J.Bravo et al. (1998). Crystal structure of a cytokine-binding region of gp130. EMBO J, 17, 1665-1674. PubMed id: 9501088 DOI: 10.1093/emboj/17.6.1665

Date:

18-Aug-98 Release date: 26-Aug-98

Protein chains

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

Seq: 918 a.a.

Struc: 208 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

DOI no: 10.1093/emboj/17.6.1665

EMBO J 17:1665-1674 (1998)

PubMed id: 9501088

Crystal structure of a cytokine-binding region of gp130.

J.Bravo, D.Staunton, J.K.Heath, E.Y.Jones.

ABSTRACT

The structure of the cytokine-binding homology region of the cell surface receptor gp130 has been determined by X-ray crystallography at 2.0 A resolution. The beta sandwich structure of the two domains conforms to the topology of the cytokine receptor superfamily. This first structure of an uncomplexed receptor exhibits a similar L-shaped quaternary structure to that of ligand-bound family members and suggests a limited flexibility in relative domain orientation of some 3 degrees. The putative ligand-binding loops are relatively rigid, with a phenylalanine side chain similarly positioned to exposed aromatic residues implicated in ligand binding for other such receptors. The positioning and structure of the N-terminal portion of the polypeptide chain have implications for the structure and function of cytokine receptors, such as gp130, which contain an additional N-terminal immunoglobulin-like domain.

Selected figure(s)

Figure 3.
Figure 3 Gp130-CHR domain 2 and interdomain linker. (A) Schematic diagram of the WSXWS box. The side chains of residues contributing to this structural feature are colour coded according to the secondary structure element from which they originate. (B) Atomic coordinates and electron density map for the WSXWS box. The refined coordinates are displayed with the original 2.9 Å resolution electron density map calculated using MAD phases followed by density modification (program DM, see Materials and methods). The map is contoured at 1 in program O. (C) Schematic diagram of the D1 -D2 linker region. Strand L in the linker region hydrogen-bonds to strand A in DL and the WSXWS box region of the polypeptide chain prior to the start of strand G in D2.

Figure 5.
Figure 5 The putative ligand-binding region in gp130-CHR compared with hGHR. Two orthogonal views are shown for gp130-CHR (green) and hGHR (yellow). Loops implicated in ligand binding for the hGH -hGHR complex, and their equivalents in the gp130-CHR structure, are denoted in red. The side chains of the structurally equivalent residues Phe169 and Trp104 are shown in ball and stick representation.

The above figures are reprinted from an Open Access publication published by Macmillan Publishers Ltd: EMBO J (1998, 17, 1665-1674) copyright 1998.

Figures were selected by an automated process.