PDBsum entry 4zne

Immune system

PDB id: 4zne

Contents

Protein chains

242 a.a.

215 a.a.

Ligands

NAG-NAG-MAN

NAG-MAN

NAG-NAG

NAG-NAG-MAN-MAN-NAG-MAN-NAG-FUL ×2

NAG ×2

Metals

_ZN ×3

Waters ×135

PDB id:

4zne

Name:

Immune system

Title:

Igg1 fc-fcgammari ecd complex

Structure:

High affinity immunoglobulin gamma fc receptor i. Chain: a. Fragment: unp residues 16-282. Synonym: igg fc receptor i,fc-gamma ri,fcri,fc-gamma ria,fcgammaria. Engineered: yes. Ig gamma-1 chain c region. Chain: e, j. Fragment: unp residues 104-330. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: fcgr1a, fcg1, fcgr1, igfr1. Expressed in: mammalian expression vector pck146. Expression_system_taxid: 943932. Gene: ighg1. Expressed in: mammalian expression vector pbgsa. Expression_system_taxid: 285261

Resolution:

2.42Å R-factor: 0.203 R-free: 0.254

Authors:

V.Y.Oganesyan,W.F.Dall'Acqua

Key ref:

V.Oganesyan et al. (2015). Structural insights into the interaction of human IgG1 with FcγRI: no direct role of glycans in binding. Acta Crystallogr D Biol Crystallogr, 71, 2354-2361. PubMed id: 26527150 DOI: 10.1107/S1399004715018015

Date:

04-May-15 Release date: 11-Nov-15

Protein chain

P12314  (FCGR1_HUMAN) -  High affinity immunoglobulin gamma Fc receptor I from Homo sapiens

Seq: 374 a.a.

Struc: 242 a.a.

Protein chains

P01857  (IGHG1_HUMAN) -  Immunoglobulin heavy constant gamma 1 from Homo sapiens

Seq: 399 a.a.

Struc: 215 a.a.*

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

DOI no: 10.1107/S1399004715018015

Acta Crystallogr D Biol Crystallogr 71:2354-2361 (2015)

PubMed id: 26527150

Structural insights into the interaction of human IgG1 with FcγRI: no direct role of glycans in binding.

V.Oganesyan, Y.Mazor, C.Yang, K.E.Cook, R.M.Woods, A.Ferguson, M.A.Bowen, T.Martin, J.Zhu, H.Wu, W.F.Dall'Acqua.

ABSTRACT

The three-dimensional structure of a human IgG1 Fc fragment bound to wild-type human FcγRI is reported. The structure of the corresponding complex was solved at a resolution of 2.4 Å using molecular replacement; this is the highest resolution achieved for an unmutated FcγRI molecule. This study highlights the critical structural and functional role played by the second extracellular subdomain of FcγRI. It also explains the long-known major energetic contribution of the Fc `LLGG' motif at positions 234-237, and particularly of Leu235, via a `lock-and-key' mechanism. Finally, a previously held belief is corrected and a differing view is offered on the recently proposed direct role of Fc carbohydrates in the corresponding interaction. Structural evidence is provided that such glycan-related effects are strictly indirect.