3KBH

Crystal structure of NL63 respiratory coronavirus receptor-binding domain complexed with its human receptor

Summary for 3KBH

• Entry DOI: 10.2210/pdb3kbh/pdb
• Related: 2AJF
• Descriptor: Angiotensin-converting enzyme 2, Spike glycoprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total)
• Functional Keywords: beta sandwich, envelope protein, fusion protein, glycoprotein, host-virus interaction, membrane, transmembrane, virion, virulence, carboxypeptidase, cell membrane, chloride, metal-binding, metalloprotease, protease, secreted, hydrolase
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 8
• Total formula weight: 340261.37

Authors

Wu, K.,Li, W.,Peng, G.,Li, F. (deposition date: 2009-10-20, release date: 2009-12-15, Last modification date: 2024-11-27)

Primary citation

Wu, K.,Li, W.,Peng, G.,Li, F.
Crystal structure of NL63 respiratory coronavirus receptor-binding domain complexed with its human receptor.
Proc.Natl.Acad.Sci.USA, 106:19970-19974, 2009

PubMed Abstract: NL63 coronavirus (NL63-CoV), a prevalent human respiratory virus, is the only group I coronavirus known to use angiotensin-converting enzyme 2 (ACE2) as its receptor. Incidentally, ACE2 is also used by group II SARS coronavirus (SARS-CoV). We investigated how different groups of coronaviruses recognize the same receptor, whereas homologous group I coronaviruses recognize different receptors. We determined the crystal structure of NL63-CoV spike protein receptor-binding domain (RBD) complexed with human ACE2. NL63-CoV RBD has a novel beta-sandwich core structure consisting of 2 layers of beta-sheets, presenting 3 discontinuous receptor-binding motifs (RBMs) to bind ACE2. NL63-CoV and SARS-CoV have no structural homology in RBD cores or RBMs; yet the 2 viruses recognize common ACE2 regions, largely because of a "virus-binding hotspot" on ACE2. Among group I coronaviruses, RBD cores are conserved but RBMs are variable, explaining how these viruses recognize different receptors. These results provide a structural basis for understanding viral evolution and virus-receptor interactions.

PubMed: 19901337
DOI: 10.1073/pnas.0908837106

Experimental method

X-RAY DIFFRACTION (3.31 Å)