6pdl

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

spinqualitylabelsall models 6pdl, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6pdl is a 8 chain structure with sequence from Henipavirus hendraense and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.7Å Ligands: BMA, FUC, MAN, NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function GLYCP_HENDH Attaches the virus to sialic acid-containing cell receptors and thereby initiating infection. Binding of glycoprotein G to the receptor induces a conformational change that allows the F protein to trigger virion/cell membranes fusion (By similarity). Publication Abstract from PubMed 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. New insights into the Hendra virus attachment and entry process from structures of the virus G glycoprotein and its complex with Ephrin-B2.,Xu K, Chan YP, Rajashankar KR, Khetawat D, Yan L, Kolev MV, Broder CC, Nikolov DB PLoS One. 2012;7(11):e48742. doi: 10.1371/journal.pone.0048742. Epub 2012 Nov 5. PMID:23144952 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Ephrin

Proteopedia Page Contributors and Editors (what is this?)

OCA