1PIV

BINDING OF THE ANTIVIRAL DRUG WIN51711 TO THE SABIN STRAIN OF TYPE 3 POLIOVIRUS: STRUCTURAL COMPARISON WITH DRUG BINDING IN RHINOVIRUS 14


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.90 Å
  • R-Value Observed: 0.316 

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This is version 1.2 of the entry. See complete history


Literature

Binding of the antiviral drug WIN51711 to the sabin strain of type 3 poliovirus: structural comparison with drug binding in rhinovirus 14.

Hiremath, C.N.Grant, R.A.Filman, D.J.Hogle, J.M.

(1995) Acta Crystallogr D Biol Crystallogr 51: 473-489

  • DOI: https://doi.org/10.1107/S090744499401084X
  • Primary Citation of Related Structures:  
    1PIV

  • PubMed Abstract: 

    The crystal structure of the Sabin strain of type 3 poliovirus (P3/Sabin) complexed with the antiviral drug WIN51711 has been determined at 2.9 A resolution. Drugs of this kind are known to inhibit the uncoating of the virus during infection, by stabilizing the capsid against receptor-induced conformational changes. The electron density for the bound drug is very well defined so that its position and orientation are unambiguous. The drug binds in a nearly extended conformation, slightly bent in the middle, in a blind pocket formed predominantly by hydrophobic residues in the core of the beta-barrel of capsid protein VP1. Comparisons between this structure, the corresponding drug complex in human rhinovirus 14 (HRV 14), and the native structures of both viruses demonstrate that the binding of WIN51711 has markedly different effects on the structures of these two viruses. Unlike HRV14, wherein large conformational changes are observed in the coat protein after drug binding, the binding of this drug in poliovirus does not induce any significant conformational changes in the structure of the capsid protein, though the drug has a greater inhibitory effect in P3/Sabin than in HRV14. The implications of this result for the mechanism of capsid stabilization are discussed.


  • Organizational Affiliation

    Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.


Macromolecules

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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
POLIOVIRUS TYPE 3 (SUBUNIT VP1)A [auth 0]4Poliovirus type 3 (strains P3/LEON/37 AND P3/LEON 12A[1]B)Mutation(s): 0 
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
POLIOVIRUS TYPE 3 (SUBUNIT VP1)B [auth 1]301Poliovirus type 3 (strains P3/LEON/37 AND P3/LEON 12A[1]B)Mutation(s): 0 
UniProt
Find proteins for P03302 (Poliovirus type 3 (strains P3/Leon/37 and P3/Leon 12A[1]B))
Explore P03302 
Go to UniProtKB:  P03302
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP03302
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
POLIOVIRUS TYPE 3 (SUBUNIT VP2)C [auth 2]271Poliovirus type 3 (strains P3/LEON/37 AND P3/LEON 12A[1]B)Mutation(s): 0 
UniProt
Find proteins for P03302 (Poliovirus type 3 (strains P3/Leon/37 and P3/Leon 12A[1]B))
Explore P03302 
Go to UniProtKB:  P03302
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Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP03302
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
POLIOVIRUS TYPE 3 (SUBUNIT VP3)D [auth 3]238Poliovirus type 3 (strains P3/LEON/37 AND P3/LEON 12A[1]B)Mutation(s): 0 
UniProt
Find proteins for P03302 (Poliovirus type 3 (strains P3/Leon/37 and P3/Leon 12A[1]B))
Explore P03302 
Go to UniProtKB:  P03302
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UniProt GroupP03302
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Entity ID: 5
MoleculeChains Sequence LengthOrganismDetailsImage
POLIOVIRUS TYPE 3 (SUBUNIT VP4)E [auth 4]68Poliovirus type 3 (strains P3/LEON/37 AND P3/LEON 12A[1]B)Mutation(s): 0 
UniProt
Find proteins for P03302 (Poliovirus type 3 (strains P3/Leon/37 and P3/Leon 12A[1]B))
Explore P03302 
Go to UniProtKB:  P03302
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Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP03302
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Small Molecules
Ligands 2 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
W71
Query on W71

Download Ideal Coordinates CCD File 
F [auth 1]5-(7-(4-(4,5-DIHYDRO-2-OXAZOLYL)PHENOXY)HEPTYL)-3-METHYL ISOXAZOLE
C20 H26 N2 O3
FKLJPTJMIBLJAV-UHFFFAOYSA-N
MYR
Query on MYR

Download Ideal Coordinates CCD File 
G [auth 4]MYRISTIC ACID
C14 H28 O2
TUNFSRHWOTWDNC-UHFFFAOYSA-N
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.90 Å
  • R-Value Observed: 0.316 
  • Space Group: I 2 2 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 321.06α = 90
b = 358.62β = 90
c = 381.82γ = 90
Software Package:
Software NamePurpose
X-PLORmodel building
X-PLORrefinement
X-PLORphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 1995-06-03
    Type: Initial release
  • Version 1.1: 2008-03-24
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance