4L3N

Crystal structure of the receptor-binding domain from newly emerged Middle East respiratory syndrome coronavirus

Summary for 4L3N

• Entry DOI: 10.2210/pdb4l3n/pdb
• Descriptor: S protein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 1,2-ETHANEDIOL, ... (4 entities in total)
• Functional Keywords: beta-sheet fold, viral protein
• Biological source: Human betacoronavirus 2c Jordan-N3/2012
• Total number of polymer chains: 2
• Total formula weight: 49711.76

Authors

Chen, Y.,Rajashankar, K.R.,Yang, Y.,Agnihothram, S.S.,Liu, C.,Lin, Y.-L.,Baric, R.S.,Li, F. (deposition date: 2013-06-06, release date: 2013-07-31, Last modification date: 2024-10-30)

Primary citation

Chen, Y.,Rajashankar, K.R.,Yang, Y.,Agnihothram, S.S.,Liu, C.,Lin, Y.L.,Baric, R.S.,Li, F.
Crystal structure of the receptor-binding domain from newly emerged middle East respiratory syndrome coronavirus.
J.Virol., 87:10777-10783, 2013

PubMed Abstract: The newly emerged Middle East respiratory syndrome coronavirus (MERS-CoV) has infected at least 77 people, with a fatality rate of more than 50%. Alarmingly, the virus demonstrates the capability of human-to-human transmission, raising the possibility of global spread and endangering world health and economy. Here we have identified the receptor-binding domain (RBD) from the MERS-CoV spike protein and determined its crystal structure. This study also presents a structural comparison of MERS-CoV RBD with other coronavirus RBDs, successfully positioning MERS-CoV on the landscape of coronavirus evolution and providing insights into receptor binding by MERS-CoV. Furthermore, we found that MERS-CoV RBD functions as an effective entry inhibitor of MERS-CoV. The identified MERS-CoV RBD may also serve as a potential candidate for MERS-CoV subunit vaccines. Overall, this study enhances our understanding of the evolution of coronavirus RBDs, provides insights into receptor recognition by MERS-CoV, and may help control the transmission of MERS-CoV in humans.

PubMed: 23903833
DOI: 10.1128/JVI.01756-13

Experimental method

X-RAY DIFFRACTION (2.13 Å)