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	Molecular basis of Coxsackievirus A10 entry using the two-in-one attachment and uncoating receptor KRM1.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 117, Issue 31, Page 18711-18718, Year 2020
Publish date	Aug 4, 2020
Authors	Yingzi Cui / Ruchao Peng / Hao Song / Zhou Tong / Xiao Qu / Sheng Liu / Xin Zhao / Yan Chai / Peiyi Wang / George F Gao / Jianxun Qi /
PubMed Abstract	KREMEN1 (KRM1) has been identified as a functional receptor for Coxsackievirus A10 (CV-A10), a causative agent of hand-foot-and-mouth disease (HFMD), which poses a great threat to infants globally. ...KREMEN1 (KRM1) has been identified as a functional receptor for Coxsackievirus A10 (CV-A10), a causative agent of hand-foot-and-mouth disease (HFMD), which poses a great threat to infants globally. However, the underlying mechanisms for the viral entry process are not well understood. Here we determined the atomic structures of different forms of CV-A10 viral particles and its complex with KRM1 in both neutral and acidic conditions. These structures reveal that KRM1 selectively binds to the mature viral particle above the canyon of the viral protein 1 (VP1) subunit and contacts across two adjacent asymmetry units. The key residues for receptor binding are conserved among most KRM1-dependent enteroviruses, suggesting a uniform mechanism for receptor binding. Moreover, the binding of KRM1 induces the release of pocket factor, a process accelerated under acidic conditions. Further biochemical studies confirmed that receptor binding at acidic pH enabled CV-A10 virion uncoating in vitro. Taken together, these findings provide high-resolution snapshots of CV-A10 entry and identify KRM1 as a two-in-one receptor for enterovirus infection.
External links	Proc Natl Acad Sci U S A / PubMed:32690697 / PubMed Central
Methods	EM (single particle)
Resolution	3.0 - 3.6 Å
Structure data	30253 7bzn EMDB-30253, PDB-7bzn: Cryo-EM structure of mature Coxsackievirus A10 at pH 7.4 Method: EM (single particle) / Resolution: 3.1 Å 30254 7bzo EMDB-30254, PDB-7bzo: Cryo-EM structure of mature Coxsackievirus A10 at pH 5.5 Method: EM (single particle) / Resolution: 3.2 Å 30259 7bzt EMDB-30259, PDB-7bzt: Cryo-EM structure of mature Coxsackievirus A10 in complex with KRM1 at pH 7.4 Method: EM (single particle) / Resolution: 3.0 Å 30260 7bzu EMDB-30260, PDB-7bzu: Cryo-EM structure of mature Coxsackievirus A10 in complex with KRM1 at pH 5.5 Method: EM (single particle) / Resolution: 3.0 Å 30287 7c4t EMDB-30287, PDB-7c4t: Cryo-EM structure of A particle Coxsackievirus A10 at pH 7.4 Method: EM (single particle) / Resolution: 3.6 Å 30290 7c4w EMDB-30290, PDB-7c4w: Cryo-EM structure of A particle Coxsackievirus A10 at pH 5.5 Method: EM (single particle) / Resolution: 3.4 Å 30291 7c4y EMDB-30291, PDB-7c4y: Cryo-EM structure of empty Coxsackievirus A10 at pH 7.4 Method: EM (single particle) / Resolution: 3.5 Å 30292 7c4z EMDB-30292, PDB-7c4z: Cryo-EM structure of empty Coxsackievirus A10 at pH 5.5 Method: EM (single particle) / Resolution: 3.3 Å
Chemicals	ChemComp-SPH: SPHINGOSINE / Sphingosine ChemComp-NAG: 2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine
Source	coxsackievirus a10 homo sapiens (human)
Keywords	VIRUS / Picornavirus / Coxsackievirus A10 / pH 7.4 / mature particle / pH 5.5 / KRM1 / complex / A particle / empty particle