5KWB

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

Summary for 5KWB

• Entry DOI: 10.2210/pdb5kwb/pdb
• Related PRD ID: PRD_900003
• Descriptor: Spike glycoprotein, beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: coronavirus spike protein, s1-ctd, receptor binding domain, receptor binding motif, virus entry, hku1, viral protein
• Biological source: Human coronavirus HKU1 (isolate N1) (HCoV-HKU1)
• Cellular location: Spike protein S2: Virion membrane ; Single-pass type I membrane protein . Spike protein S1: Virion membrane ; Peripheral membrane protein : Q5MQD0
• Total number of polymer chains: 1
• Total formula weight: 42798.02

Authors

Guan, H.,Wojdyla, J.A.,Wang, M.,Cui, S. (deposition date: 2016-07-17, release date: 2017-06-07, Last modification date: 2024-11-06)

Primary citation

Ou, X.,Guan, H.,Qin, B.,Mu, Z.,Wojdyla, J.A.,Wang, M.,Dominguez, S.R.,Qian, Z.,Cui, S.
Crystal structure of the receptor binding domain of the spike glycoprotein of human betacoronavirus HKU1
Nat Commun, 8:15216-15216, 2017

PubMed Abstract: 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 β-CoVs to bind to its yet unknown human receptor. Here we present the crystal structure of HKU1 CTD at 1.9 Å 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 β-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.

PubMed: 28534504
DOI: 10.1038/ncomms15216

Experimental method

X-RAY DIFFRACTION (1.91 Å)