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6P7Y

Crystal Structure of the Cedar henipavirus Attachment G Glycoprotein globular domain in complex with the receptor ephrin-B2

Summary for 6P7Y
Entry DOI10.2210/pdb6p7y/pdb
DescriptorAttachment glycoprotein, Ephrin-B2, beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (9 entities in total)
Functional Keywordscedar virus, attachment, glycoprotein, g protein, viral protein, receptor, ephrin-b2, henipavirus
Biological sourceCedar virus
More
Total number of polymer chains4
Total formula weight140072.23
Authors
Xu, K.,Nikolov, D.B.,Xu, Y. (deposition date: 2019-06-06, release date: 2019-09-25, Last modification date: 2020-07-29)
Primary citationLaing, E.D.,Navaratnarajah, C.K.,Cheliout Da Silva, S.,Petzing, S.R.,Xu, Y.,Sterling, S.L.,Marsh, G.A.,Wang, L.F.,Amaya, M.,Nikolov, D.B.,Cattaneo, R.,Broder, C.C.,Xu, K.
Structural and functional analyses reveal promiscuous and species specific use of ephrin receptors by Cedar virus.
Proc.Natl.Acad.Sci.USA, 116:20707-20715, 2019
Cited by
PubMed Abstract: Cedar virus (CedV) is a bat-borne henipavirus related to Nipah virus (NiV) and Hendra virus (HeV), zoonotic agents of fatal human disease. CedV receptor-binding protein (G) shares only ∼30% sequence identity with those of NiV and HeV, although they can all use ephrin-B2 as an entry receptor. We demonstrate that CedV also enters cells through additional B- and A-class ephrins (ephrin-B1, ephrin-A2, and ephrin-A5) and report the crystal structure of the CedV G ectodomain alone and in complex with ephrin-B1 or ephrin-B2. The CedV G receptor-binding site is structurally distinct from other henipaviruses, underlying its capability to accommodate additional ephrin receptors. We also show that CedV can enter cells through mouse ephrin-A1 but not human ephrin-A1, which differ by 1 residue in the key contact region. This is evidence of species specific ephrin receptor usage by a henipavirus, and implicates additional ephrin receptors in potential zoonotic transmission.
PubMed: 31548390
DOI: 10.1073/pnas.1911773116
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.844 Å)
Structure validation

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