Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	TMPRSS2 and glycan receptors synergistically facilitate coronavirus entry.
Journal, issue, pages	Cell, Vol. 187, Issue 16, Page 4261-4271.e17, Year 2024
Publish date	Aug 8, 2024
Authors	Haofeng Wang / Xiaoce Liu / Xiang Zhang / Zhuoqian Zhao / Yuchi Lu / Dingzhe Pu / Zeyang Zhang / Jie Chen / Yajie Wang / Mengfei Li / Xuxue Dong / Yinkai Duan / Yujia He / Qiyu Mao / Hangtian Guo / Haoran Sun / Yihan Zhou / Qi Yang / Yan Gao / Xiuna Yang / Hongzhi Cao / Luke Guddat / Lei Sun / Zihe Rao / Haitao Yang /
PubMed Abstract	The entry of coronaviruses is initiated by spike recognition of host cellular receptors, involving proteinaceous and/or glycan receptors. Recently, TMPRSS2 was identified as the proteinaceous ...The entry of coronaviruses is initiated by spike recognition of host cellular receptors, involving proteinaceous and/or glycan receptors. Recently, TMPRSS2 was identified as the proteinaceous receptor for HCoV-HKU1 alongside sialoglycan as a glycan receptor. However, the underlying mechanisms for viral entry remain unknown. Here, we investigated the HCoV-HKU1C spike in the inactive, glycan-activated, and functionally anchored states, revealing that sialoglycan binding induces a conformational change of the NTD and promotes the neighboring RBD of the spike to open for TMPRSS2 recognition, exhibiting a synergistic mechanism for the entry of HCoV-HKU1. The RBD of HCoV-HKU1 features an insertion subdomain that recognizes TMPRSS2 through three previously undiscovered interfaces. Furthermore, structural investigation of HCoV-HKU1A in combination with mutagenesis and binding assays confirms a conserved receptor recognition pattern adopted by HCoV-HKU1. These studies advance our understanding of the complex viral-host interactions during entry, laying the groundwork for developing new therapeutics against coronavirus-associated diseases.
External links	Cell / PubMed:38964329
Methods	EM (single particle)
Resolution	2.95 - 3.65 Å
Structure data	39025 8y7x EMDB-39025, PDB-8y7x: Structure of HCoV-HKU1A spike in the functionally anchored-3up conformation with 3TMPRSS2 Method: EM (single particle) / Resolution: 3.09 Å 39026 8y7y EMDB-39026, PDB-8y7y: Local structure of HCoV-HKU1A spike in complex with TMPRSS2 and glycan Method: EM (single particle) / Resolution: 3.24 Å 39036 8y87 EMDB-39036, PDB-8y87: Structure of HCoV-HKU1C spike in the functionally anchored-1up conformation with 1TMPRSS2 Method: EM (single particle) / Resolution: 3.26 Å 39037 8y88 EMDB-39037, PDB-8y88: Structure of HCoV-HKU1C spike in the functionally anchored-2up conformation with 2TMPRSS2 Method: EM (single particle) / Resolution: 3.03 Å 39038 8y89 EMDB-39038, PDB-8y89: Structure of HCoV-HKU1C spike in the functionally anchored-3up conformation with 2TMPRSS2 Method: EM (single particle) / Resolution: 3.32 Å 39039 8y8a EMDB-39039, PDB-8y8a: Structure of HCoV-HKU1C spike in the functionally anchored-3up conformation with 3TMPRSS2 Method: EM (single particle) / Resolution: 3.19 Å 39040 8y8b EMDB-39040, PDB-8y8b: Local structure of HCoV-HKU1C spike in complex with TMPRSS2 and glycan Method: EM (single particle) / Resolution: 3.01 Å 39041 8y8c EMDB-39041, PDB-8y8c: Structure of HCoV-HKU1C spike in the inactive-closed conformation Method: EM (single particle) / Resolution: 2.95 Å 39042 8y8d EMDB-39042, PDB-8y8d: Structure of HCoV-HKU1C spike in the inactive-1up conformation Method: EM (single particle) / Resolution: 3.41 Å 39043 8y8e EMDB-39043, PDB-8y8e: Structure of HCoV-HKU1C spike in the inactive-2up conformation Method: EM (single particle) / Resolution: 3.62 Å 39044 8y8f EMDB-39044, PDB-8y8f: Structure of HCoV-HKU1C spike in the glycan-activated-closed conformation Method: EM (single particle) / Resolution: 3.07 Å 39045 8y8g EMDB-39045, PDB-8y8g: Structure of HCoV-HKU1C spike in the glycan-activated-1up conformation Method: EM (single particle) / Resolution: 3.23 Å 39046 8y8h EMDB-39046, PDB-8y8h: Structure of HCoV-HKU1C spike in the glycan-activated-2up conformation Method: EM (single particle) / Resolution: 3.65 Å 39047 8y8i EMDB-39047, PDB-8y8i: Structure of HCoV-HKU1C spike in the glycan-activated-3up conformation Method: EM (single particle) / Resolution: 3.58 Å 39048 8y8j EMDB-39048, PDB-8y8j: Local structure of HCoV-HKU1C spike in complex with glycan Method: EM (single particle) / Resolution: 3.57 Å
Chemicals	ChemComp-NAG: 2-acetamido-2-deoxy-beta-D-glucopyranose ChemComp-MJJ: methyl 9-O-acetyl-5-acetamido-3,5-dideoxy-D-glycero-alpha-D-galacto-non-2-ulopyranosidonic acid
Source	human coronavirus hku1 human coronavirus hku1 (isolate n1) homo sapiens (human) human coronavirus hku1 (isolate n5)
Keywords	VIRAL PROTEIN / HKU1A / spike / TMPRSS2 / HKU1C