3R4D

Crystal structure of mouse coronavirus receptor-binding domain complexed with its murine receptor

Summary for 3R4D

• Entry DOI: 10.2210/pdb3r4d/pdb
• Related: 1L6Z 2ajf 3kbh
• Descriptor: CEA-related cell adhesion molecule 1, isoform 1/2S, Spike glycoprotein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: immunoglobulin, beta-sandwich, mceacam1a - immunoglobulin fold mhv spike ntd - galectin-like beta-sandwich fold, mceacam1a - cell adhesion mhv spike ntd - mceacam1a binding, mceacam1a - itself and mhv spike ntd mhv spike ntd - mceacam1a, n-glycosylations, mceacam1a - 37, 55, 70 mhv spike ntd - 192, cell adhesion-viral protein complex, cell adhesion/viral protein
• Biological source: Mus musculus (Mouse); More
• Total number of polymer chains: 4
• Total formula weight: 114104.39

Authors

Peng, G.Q.,Sun, D.W.,Rajashankar, K.R.,Qian, Z.H.,Holmes, K.V.,Li, F. (deposition date: 2011-03-17, release date: 2011-06-22, Last modification date: 2024-10-16)

Primary citation

Peng, G.,Sun, D.,Rajashankar, K.R.,Qian, Z.,Holmes, K.V.,Li, F.
Crystal structure of mouse coronavirus receptor-binding domain complexed with its murine receptor.
Proc.Natl.Acad.Sci.USA, 108:10696-10701, 2011

PubMed Abstract: Coronaviruses have evolved diverse mechanisms to recognize different receptors for their cross-species transmission and host-range expansion. Mouse hepatitis coronavirus (MHV) uses the N-terminal domain (NTD) of its spike protein as its receptor-binding domain. Here we present the crystal structure of MHV NTD complexed with its receptor murine carcinoembryonic antigen-related cell adhesion molecule 1a (mCEACAM1a). Unexpectedly, MHV NTD contains a core structure that has the same β-sandwich fold as human galectins (S-lectins) and additional structural motifs that bind to the N-terminal Ig-like domain of mCEACAM1a. Despite its galectin fold, MHV NTD does not bind sugars, but instead binds mCEACAM1a through exclusive protein-protein interactions. Critical contacts at the interface have been confirmed by mutagenesis, providing a structural basis for viral and host specificities of coronavirus/CEACAM1 interactions. Sugar-binding assays reveal that galectin-like NTDs of some coronaviruses such as human coronavirus OC43 and bovine coronavirus bind sugars. Structural analysis and mutagenesis localize the sugar-binding site in coronavirus NTDs to be above the β-sandwich core. We propose that coronavirus NTDs originated from a host galectin and retained sugar-binding functions in some contemporary coronaviruses, but evolved new structural features in MHV for mCEACAM1a binding.

PubMed: 21670291
DOI: 10.1073/pnas.1104306108

Experimental method

X-RAY DIFFRACTION (3.1 Å)