6thb

Receptor binding domain of the Cedar Virus attachment glycoprotein (G)

spinqualitylabelsall models 6thb, resolution 2.78Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6thb is a 2 chain structure with sequence from Cedpv. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: NAG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed The emergent zoonotic henipaviruses, Hendra, and Nipah are responsible for frequent and fatal disease outbreaks in domestic animals and humans. Specificity of henipavirus attachment glycoproteins (G) for highly species-conserved ephrin ligands underpins their broad host range and is associated with systemic and neurological disease pathologies. Here, we demonstrate that Cedar virus (CedV)-a related henipavirus that is ostensibly nonpathogenic-possesses an idiosyncratic entry receptor repertoire that includes the common henipaviral receptor, ephrin-B2, but, distinct from pathogenic henipaviruses, does not include ephrin-B3. Uniquely among known henipaviruses, CedV can use ephrin-B1 for cellular entry. Structural analyses of CedV-G reveal a key region of molecular specificity that directs ephrin-B1 utilization, while preserving a universal mode of ephrin-B2 recognition. The structural and functional insights presented uncover diversity within the known henipavirus receptor repertoire and suggest that only modest structural changes may be required to modulate receptor specificities within this group of lethal human pathogens. A key region of molecular specificity orchestrates unique ephrin-B1 utilization by Cedar virus.,Pryce R, Azarm K, Rissanen I, Harlos K, Bowden TA, Lee B Life Sci Alliance. 2019 Dec 20;3(1). pii: 3/1/e201900578. doi:, 10.26508/lsa.201900578. Print 2020 Jan. PMID:31862858 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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