PDBsum entry 2y7q

Immune system

PDB id: 2y7q

Contents

Protein chains

158 a.a.

287 a.a.

290 a.a.

Ligands

NAG-NAG-BMA-MAN

NAG ×3

PDB id:

2y7q

Name:

Immune system

Title:

The high-affinity complex between ige and its receptor fc epsilon ri

Structure:

High affinity immunoglobulin epsilon receptor subunit alpha. Chain: a. Fragment: soluble extracellular domains, residues 26-201. Synonym: high affinity ige receptor fc epsilon ri, ige fc receptor subunit alpha, fc-epsilon ri-alpha, fceri. Engineered: yes. Mutation: yes. Ig epsilon chain c region.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: hek293s. Expressed in: mus musculus. Expression_system_taxid: 10090. Expression_system_cell_line: mouse myeloma ns0.

Resolution:

3.40Å R-factor: 0.248 R-free: 0.292

Authors:

A.M.Davies,M.D.Holdom,J.E.Nettleship,A.J.Beavil,R.J.Owens,B.J.Sutton

Key ref:

M.D.Holdom et al. (2011). Conformational changes in IgE contribute to its uniquely slow dissociation rate from receptor FcɛRI. Nat Struct Biol, 18, 571-576. PubMed id: 21516097

Date:

01-Feb-11 Release date: 20-Apr-11

Protein chain

P12319  (FCERA_HUMAN) -  High affinity immunoglobulin epsilon receptor subunit alpha from Homo sapiens

Seq: 257 a.a.

Struc: 158 a.a.*

Protein chain

P01854  (IGHE_HUMAN) -  Immunoglobulin heavy constant epsilon from Homo sapiens

Seq: 546 a.a.

Struc: 287 a.a.*

Protein chain

P01854  (IGHE_HUMAN) -  Immunoglobulin heavy constant epsilon from Homo sapiens

Seq: 546 a.a.

Struc: 290 a.a.*

* PDB and UniProt seqs differ at 8 residue positions (black crosses)

Nat Struct Biol 18:571-576 (2011)

PubMed id: 21516097

Conformational changes in IgE contribute to its uniquely slow dissociation rate from receptor FcɛRI.

M.D.Holdom, A.M.Davies, J.E.Nettleship, S.C.Bagby, B.Dhaliwal, E.Girardi, J.Hunt, H.J.Gould, A.J.Beavil, J.M.McDonnell, R.J.Owens, B.J.Sutton.

ABSTRACT

No abstract given.