6PDL

Crystal Structure of Hendra Virus Attachment G Glycoprotein in Complex with Receptor Ephrin-B2

Summary for 6PDL

• Entry DOI: 10.2210/pdb6pdl/pdb
• Descriptor: Attachment glycoprotein, Ephrin-B2, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (9 entities in total)
• Functional Keywords: attachment, glycoprotein, g protein, viral protein, receptor, viral protein-signaling protein complex, viral protein/signaling protein
• Biological source: Hendra henipavirus; More
• Total number of polymer chains: 8
• Total formula weight: 273221.29

Authors

Xu, K.,Nikolov, D.B. (deposition date: 2019-06-19, release date: 2019-11-27, Last modification date: 2024-10-30)

Primary citation

Xu, K.,Chan, Y.P.,Rajashankar, K.R.,Khetawat, D.,Yan, L.,Kolev, M.V.,Broder, C.C.,Nikolov, D.B.
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-, 2012

PubMed 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.

PubMed: 23144952
DOI: 10.1371/journal.pone.0048742

Experimental method

X-RAY DIFFRACTION (2.7 Å)