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6JO8

The complex structure of CHIKV envelope glycoprotein bound to human MXRA8

Summary for 6JO8
Entry DOI10.2210/pdb6jo8/pdb
DescriptorTogavirin, CHIKV E1, Matrix remodeling-associated protein 8, ... (5 entities in total)
Functional Keywordsarthritogenic alphaviruses, receptor, mxra8, chikungunya virus, viral protein
Biological sourceChikungunya virus (CHIKV)
More
Total number of polymer chains9
Total formula weight367679.12
Authors
Song, H.,Zhao, Z.,Qi, J.,Gao, F.,Gao, F.G. (deposition date: 2019-03-20, release date: 2019-05-15, Last modification date: 2024-11-20)
Primary citationSong, H.,Zhao, Z.,Chai, Y.,Jin, X.,Li, C.,Yuan, F.,Liu, S.,Gao, Z.,Wang, H.,Song, J.,Vazquez, L.,Zhang, Y.,Tan, S.,Morel, C.M.,Yan, J.,Shi, Y.,Qi, J.,Gao, F.,Gao, G.F.
Molecular Basis of Arthritogenic Alphavirus Receptor MXRA8 Binding to Chikungunya Virus Envelope Protein.
Cell, 177:1714-1724.e12, 2019
Cited by
PubMed Abstract: Arthritogenic alphaviruses, such as Chikungunya virus (CHIKV), cause severe and debilitating rheumatic diseases worldwide, resulting in severe morbidity and economic costs. Recently, MXRA8 was reported as an entry receptor. Here, we present the crystal structures of the mouse MXRA8, human MXRA8 in complex with the CHIKV E protein, and the cryo-electron microscopy structure of human MXRA8 and CHIKV virus-like particle. MXRA8 has two Ig-like domains with unique structural topologies. This receptor binds in the "canyon" between two protomers of the E spike on the surface of the virion. The atomic details at the interface between the two binding entities reveal that both the two domains and the hinge region of MXRA8 are involved in interaction with CHIKV E1-E2 residues from two protomers. Notably, the stalk region of MXRA8 is critical for CHIKV virus entry. This finding provides important information regarding the development of therapeutic countermeasures against those arthritogenic alphaviruses.
PubMed: 31080063
DOI: 10.1016/j.cell.2019.04.008
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.495 Å)
Structure validation

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