PDBsum entry 6pd4

Viral protein

PDB id: 6pd4

Contents

Protein chains

436 a.a.

Ligands

NAG-NAG ×4

NAG-FUC-NAG-FUC

NAG-NAG-BMA-BMA-FUC-FUC

NAG ×2

SO4 ×13

Waters ×603

PDB id:

6pd4

Name:

Viral protein

Title:

Crystal structure of hendra virus attachment g glycoprotein

Structure:

Attachment glycoprotein. Chain: a, b. Synonym: glycoprotein. Engineered: yes

Source:

Hendra henipavirus. Organism_taxid: 63330. Expressed in: insect cell expression vector ptie1. Expression_system_taxid: 266783

Resolution:

2.20Å R-factor: 0.169 R-free: 0.207

Authors:

K.Xu,D.B.Nikolov

Key ref:

K.Xu et al. (2012). New insights into the Hendra virus attachment and entry process from structures of the virus G glycoprotein and its complex with Ephrin-B2. PLoS One, 7, e48742. PubMed id: 23144952 DOI: 10.1371/journal.pone.0048742

Date:

18-Jun-19 Release date: 27-Nov-19

Protein chains

O89343  (GLYCP_HENDH) -  Glycoprotein G from Hendra virus (isolate Horse/Autralia/Hendra/1994)

Seq: 604 a.a.

Struc: 436 a.a.

DOI no: 10.1371/journal.pone.0048742

PLoS One 7:e48742 (2012)

PubMed id: 23144952

New insights into the Hendra virus attachment and entry process from structures of the virus G glycoprotein and its complex with Ephrin-B2.

K.Xu, Y.P.Chan, K.R.Rajashankar, D.Khetawat, L.Yan, M.V.Kolev, C.C.Broder, D.B.Nikolov.

ABSTRACT

Hendra virus and Nipah virus, comprising the genus Henipavirus, are recently emerged, highly pathogenic and often lethal zoonotic agents against which there are no approved therapeutics. Two surface glycoproteins, the attachment (G) and fusion (F), mediate host cell entry. The crystal structures of the Hendra G glycoprotein alone and in complex with the ephrin-B2 receptor reveal that henipavirus uses Tryptophan 122 on ephrin-B2/B3 as a "latch" to facilitate the G-receptor association. Structural-based mutagenesis of residues in the Hendra G glycoprotein at the receptor binding interface document their importance for viral attachments and entry, and suggest that the stability of the Hendra-G-ephrin attachment complex does not strongly correlate with the efficiency of viral entry. In addition, our data indicates that conformational rearrangements of the G glycoprotein head domain upon receptor binding may be the trigger leading to the activation of the viral F fusion glycoprotein during virus infection.