5kwb

From Proteopedia

Crystal Structure of the Receptor Binding Domain of the Spike Glycoprotein of Human Betacoronavirus HKU1 (HKU1 1A-CTD, 1.9 angstrom, molecular replacement)

Structural highlights

5kwb is a 1 chain structure with sequence from Human coronavirus HKU1 (isolate N1). Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.91Å
Ligands:	, , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SPIKE_CVHN1 S1 attaches the virion to the cell membrane by interacting with cell receptors, initiating the infection. S2 is a class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and target cell membrane fusion, the coiled coil regions (heptad repeats) assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and target cell membranes. Presumably interacts with target cell lipid raft after cell attachment (By similarity).

Publication Abstract from PubMed

Human coronavirus (CoV) HKU1 is a pathogen causing acute respiratory illnesses and so far little is known about its biology. HKU1 virus uses its S1 subunit C-terminal domain (CTD) and not the N-terminal domain like other lineage A beta-CoVs to bind to its yet unknown human receptor. Here we present the crystal structure of HKU1 CTD at 1.9 A resolution. The structure consists of three subdomains: core, insertion and subdomain-1 (SD-1). While the structure of the core and SD-1 subdomains of HKU1 are highly similar to those of other beta-CoVs, the insertion subdomain adopts a novel fold, which is largely invisible in the cryo-EM structure of the HKU1 S trimer. We identify five residues in the insertion subdomain that are critical for binding of neutralizing antibodies and two residues essential for receptor binding. Our study contributes to a better understanding of entry, immunity and evolution of CoV S proteins.

Crystal structure of the receptor binding domain of the spike glycoprotein of human betacoronavirus HKU1.,Ou X, Guan H, Qin B, Mu Z, Wojdyla JA, Wang M, Dominguez SR, Qian Z, Cui S Nat Commun. 2017 May 23;8:15216. doi: 10.1038/ncomms15216. PMID:28534504^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Ou X, Guan H, Qin B, Mu Z, Wojdyla JA, Wang M, Dominguez SR, Qian Z, Cui S. Crystal structure of the receptor binding domain of the spike glycoprotein of human betacoronavirus HKU1. Nat Commun. 2017 May 23;8:15216. doi: 10.1038/ncomms15216. PMID:28534504 doi:http://dx.doi.org/10.1038/ncomms15216