Cryo-EM structures of MERS-CoV and SARS-CoV spike glycoproteins reveal the dynamic receptor binding domains

Nature Communications

Volumn 8, Issue , 2017, Pages

  Yuan, Yuan ^a,b   Cao, Duanfang ^c   Zhang, Yanfang ^b,d   Ma, Jun ^c   Qi, Jianxun ^b   Wang, Qihui ^b   Lu, Guangwen ^e   Wu, Ying ^f   Yan, Jinghua ^b,g,h,i   Shi, Yi ^b,g,h,i   Zhang, Xinzheng ^c   Gao, George F ^{a,b,d,g,h,i,j}  

^a UNIVERSITY OF SCIENCE AND TECHNOLOGY OF CHINA   (China)

^b INSTITUTE OF MICROBIOLOGY   (China)

^c INSTITUTE OF BIOPHYSICS   (China)

^d Tianjin Institute of Industrial Biotechnology   (China)

^e SICHUAN UNIVERSITY   (China)

^f WUHAN UNIVERSITY   (China)

^g SHENZHEN THIRD PEOPLE S HOSPITAL   (China)

^h INSTITUTE OF GEOLOGY AND GEOPHYSICS   (China)

ⁱ UNIVERSITY OF CHINESE ACADEMY OF SCIENCES   (China)

^j CHINESE CENTER FOR DISEASE CONTROL AND PREVENTION   (China)

more..

Author keywords

[No Author keywords available]

Indexed keywords

NEUTRALIZING ANTIBODY; VIRUS FUSION PROTEIN; VIRUS SPIKE PROTEIN; ANTIVIRUS AGENT; CORONAVIRUS SPIKE GLYCOPROTEIN; GLYCOPROTEIN; PROTEIN BINDING; S PROTEIN, SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS; VIRUS RECEPTOR;

CHEMICAL BINDING; DISEASE TREATMENT; HOST; PROTEIN; VIRAL DISEASE; VIRUS;

ARTICLE; CORONAVIRIDAE; CRYOELECTRON MICROSCOPY; HUMAN CORONAVIRUS HKU1; HUMAN CORONAVIRUS MHV; HUMAN CORONAVIRUS NL63; MIDDLE EAST RESPIRATORY SYNDROME CORONAVIRUS; MOLECULAR DYNAMICS; NONHUMAN; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN STRUCTURE; RECEPTOR BINDING; SARS CORONAVIRUS; VIRUS CELL INTERACTION; CHEMISTRY; DRUG EFFECT; GLYCOSYLATION; MEMBRANE FUSION; METABOLISM; MOLECULAR MODEL; PROTEIN MULTIMERIZATION; ULTRASTRUCTURE;

MURINE HEPATITIS VIRUS; SARS CORONAVIRUS;

ANTIBODIES, NEUTRALIZING; ANTIVIRAL AGENTS; CRYOELECTRON MICROSCOPY; GLYCOPROTEINS; GLYCOSYLATION; MEMBRANE FUSION; MIDDLE EAST RESPIRATORY SYNDROME CORONAVIRUS; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN DOMAINS; PROTEIN MULTIMERIZATION; RECEPTORS, VIRUS; SARS VIRUS; SPIKE GLYCOPROTEIN, CORONAVIRUS;

EID: 85017378927     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms15092     Document Type: Article

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