6SNW

Structure of Coxsackievirus A10 complexed with its receptor KREMEN1


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.90 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

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This is version 1.2 of the entry. See complete history


Literature

Hand-foot-and-mouth disease virus receptor KREMEN1 binds the canyon of Coxsackie Virus A10.

Zhao, Y.Zhou, D.Ni, T.Karia, D.Kotecha, A.Wang, X.Rao, Z.Jones, E.Y.Fry, E.E.Ren, J.Stuart, D.I.

(2020) Nat Commun 11: 38-38

  • DOI: https://doi.org/10.1038/s41467-019-13936-2
  • Primary Citation of Related Structures:  
    6SMG, 6SNB, 6SNW

  • PubMed Abstract: 

    Coxsackievirus A10 (CV-A10) is responsible for an escalating number of severe infections in children, but no prophylactics or therapeutics are currently available. KREMEN1 (KRM1) is the entry receptor for the largest receptor-group of hand-foot-and-mouth disease causing viruses, which includes CV-A10. We report here structures of CV-A10 mature virus alone and in complex with KRM1 as well as of the CV-A10 A-particle. The receptor spans the viral canyon with a large footprint on the virus surface. The footprint has some overlap with that seen for the neonatal Fc receptor complexed with enterovirus E6 but is larger and distinct from that of another enterovirus receptor SCARB2. Reduced occupancy of a particle-stabilising pocket factor in the complexed virus and the presence of both unbound and expanded virus particles suggests receptor binding initiates a cascade of conformational changes that produces expanded particles primed for viral uncoating.


  • Organizational Affiliation

    Division of Structural Biology, The Wellcome Centre for Human Genetics, University of Oxford, Headington, Oxford, OX3 7BN, UK.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Capsid protein VP1298Coxsackievirus A10Mutation(s): 0 
EC: 3.4.22.29 (PDB Primary Data), 3.6.1.15 (PDB Primary Data), 3.4.22.28 (PDB Primary Data), 2.7.7.48 (PDB Primary Data)
UniProt
Find proteins for Q6JKR9 (Coxsackievirus A10)
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Go to UniProtKB:  Q6JKR9
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UniProt GroupQ6JKR9
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Coxsackievirus VP2255Coxsackievirus A10Mutation(s): 0 
EC: 3.4.22.29 (PDB Primary Data), 3.6.1.15 (PDB Primary Data), 3.4.22.28 (PDB Primary Data), 2.7.7.48 (PDB Primary Data)
UniProt
Find proteins for Q6JKR9 (Coxsackievirus A10)
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Go to UniProtKB:  Q6JKR9
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UniProt GroupQ6JKR9
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Capsid protein VP3240Coxsackievirus A10Mutation(s): 0 
EC: 3.4.22.29 (PDB Primary Data), 3.6.1.15 (PDB Primary Data), 3.4.22.28 (PDB Primary Data), 2.7.7.48 (PDB Primary Data)
UniProt
Find proteins for Q6JKR9 (Coxsackievirus A10)
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Go to UniProtKB:  Q6JKR9
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UniProt GroupQ6JKR9
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
Coxsackievirus VP469Coxsackievirus A10Mutation(s): 0 
EC: 3.4.22.29 (PDB Primary Data), 3.6.1.15 (PDB Primary Data), 3.4.22.28 (PDB Primary Data), 2.7.7.48 (PDB Primary Data)
UniProt
Find proteins for Q6JKR9 (Coxsackievirus A10)
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Entity ID: 5
MoleculeChains Sequence LengthOrganismDetailsImage
Kremen protein 1378Homo sapiensMutation(s): 0 
Gene Names: KREMEN1KREMENKRM1
UniProt & NIH Common Fund Data Resources
Find proteins for Q96MU8 (Homo sapiens)
Explore Q96MU8 
Go to UniProtKB:  Q96MU8
PHAROS:  Q96MU8
GTEx:  ENSG00000183762 
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UniProt GroupQ96MU8
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Experimental Data & Validation

Experimental Data

  • Method: ELECTRON MICROSCOPY
  • Resolution: 3.90 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 
EM Software:
TaskSoftware PackageVersion
MODEL REFINEMENTPHENIX

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Medical Research Council (United Kingdom)United KingdomMR/N00065X/1
Wellcome TrustUnited Kingdom101122/Z/13/Z
Cancer Research UKUnited KingdomC375/A17721

Revision History  (Full details and data files)

  • Version 1.0: 2020-01-15
    Type: Initial release
  • Version 1.1: 2020-01-22
    Changes: Database references
  • Version 1.2: 2020-07-29
    Type: Remediation
    Reason: Carbohydrate remediation
    Changes: Data collection, Derived calculations, Structure summary