PDBsum entry 2gys

Signaling protein, cytokine

PDB id: 2gys

Contents

Protein chain

397 a.a. *

Ligands

NAG-NAG-BMA-FUC ×2

NAG-FUC-NAG ×2

* Residue conservation analysis

PDB id:

2gys

Name:

Signaling protein, cytokine

Title:

2.7 a structure of the extracellular domains of the human beta common receptor involved in il-3, il-5, and gm-csf signalling

Structure:

Cytokine receptor common beta chain. Chain: a, b. Fragment: extracellular domain, residues 25-443. Synonym: gm-csf/il-3/il-5 receptor common beta-chain, cd131 antigen, cdw131. Engineered: yes. Mutation: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: csf2rb, il3rb, il5rb. Expressed in: trichoplusia ni. Expression_system_taxid: 7111.

Biol. unit:

Dimer (from PQS)

Resolution:

2.70Å R-factor: 0.214 R-free: 0.269

Authors:

P.D.Carr,F.Conlan,S.Ford,D.L.Ollis,I.G.Young

Key ref:

P.D.Carr et al. (2006). An improved resolution structure of the human beta common receptor involved in IL-3, IL-5 and GM-CSF signalling which gives better definition of the high-affinity binding epitope. Acta Crystallograph Sect F Struct Biol Cryst Commun, 62, 509-513. PubMed id: 16754968 DOI: 10.1107/S1744309106016812

Date:

09-May-06 Release date: 20-Jun-06

Protein chains

P32927  (IL3RB_HUMAN) -  Cytokine receptor common subunit beta from Homo sapiens

Seq: 897 a.a.

Struc: 397 a.a.*

* PDB and UniProt seqs differ at 6 residue positions (black crosses)

DOI no: 10.1107/S1744309106016812

Acta Crystallograph Sect F Struct Biol Cryst Commun 62:509-513 (2006)

PubMed id: 16754968

An improved resolution structure of the human beta common receptor involved in IL-3, IL-5 and GM-CSF signalling which gives better definition of the high-affinity binding epitope.

P.D.Carr, F.Conlan, S.Ford, D.L.Ollis, I.G.Young.

ABSTRACT

X-ray diffraction has been used to produce and refine a model of the extracellular domains of the beta common cytokine receptor. A minor improvement in resolution has resulted in improved electron-density maps, which have given a clearer indication of the position and stabilization of the key residues Tyr15, Phe79, Tyr347, His349, Ile350 and Tyr403 in the elbow region between domain 1 and domain 4 of the dimer-related molecule.

Selected figure(s)

Figure 3.
Figure 3 Orthogonal views of the overlay of domain 4 from 1egj (Rossjohn et al., 2000[Rossjohn, J., McKinstry, W. J., Woodcock, J. M., McClure, B. J., Hercus, T. R., Parker, M. W., Lopez, A. F. & Bagley, C. J. (2000). Blood, 95, 2491-2498.]; red) and the current study (green). Residues implicated by mutagenesis as important in affinity conversion are shown in ball-and-stick representation (His349, Tyr347, Ile350 and Tyr403).

Figure 4.
Figure 4 Domains A1/B4 from the current study, showing the position of the residues involved in high-affinity complex formation.

The above figures are reprinted from an Open Access publication published by the IUCr: Acta Crystallograph Sect F Struct Biol Cryst Commun (2006, 62, 509-513) copyright 2006.

Figures were selected by the author.