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PDBsum entry 5w3e

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protein Protein-protein interface(s) links
Virus/immune system PDB id
5w3e

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
116 a.a.
107 a.a.
274 a.a.
236 a.a.
255 a.a.
40 a.a.
Waters ×216
PDB id:
5w3e
Name: Virus/immune system
Title: Cryoem structure of rhinovirus b14 in complex with c5 fab (33 degrees celsius, molar ratio 1:3, full particle)
Structure: C5 antibody variable heavy domain. Chain: e. C5 antibody variable light domain. Chain: g. Viral protein 1. Chain: a. Fragment: unp residues 568-856. Viral protein 3. Chain: b.
Source: Mus musculus. Mouse. Organism_taxid: 10090. Human rhinovirus 14. Hrv-14, human rhinovirus b14. Organism_taxid: 12131. Organism_taxid: 12131
Authors: Y.Liu,Y.Dong,M.G.Rossmann
Key ref: Y.Dong et al. (2017). Antibody-induced uncoating of human rhinovirus B14. Proc Natl Acad Sci U S A, 114, 8017-8022. PubMed id: 28696310
Date:
07-Jun-17     Release date:   12-Jul-17    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
No UniProt id for this chain
Struc: 116 a.a.
Protein chain
No UniProt id for this chain
Struc: 107 a.a.
Protein chain
Pfam   ArchSchema ?
P03303  (POLG_HRV14) -  Genome polyprotein from Human rhinovirus 14
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
2179 a.a.
274 a.a.
Protein chain
Pfam   ArchSchema ?
P03303  (POLG_HRV14) -  Genome polyprotein from Human rhinovirus 14
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
2179 a.a.
236 a.a.
Protein chain
Pfam   ArchSchema ?
P03303  (POLG_HRV14) -  Genome polyprotein from Human rhinovirus 14
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
2179 a.a.
255 a.a.
Protein chain
Pfam   ArchSchema ?
P03303  (POLG_HRV14) -  Genome polyprotein from Human rhinovirus 14
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
2179 a.a.
40 a.a.
Key:    PfamA domain  Secondary structure

 Enzyme reactions 
   Enzyme class 2: Chains A, B, C, D: E.C.2.7.7.48  - RNA-directed Rna polymerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate
RNA(n)
+ ribonucleoside 5'-triphosphate
= RNA(n+1)
+ diphosphate
   Enzyme class 3: Chains A, B, C, D: E.C.3.4.22.28  - picornain 3C.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
   Enzyme class 4: Chains A, B, C, D: E.C.3.4.22.29  - picornain 2A.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Selective cleavage of Tyr-|-Gly bond in the picornavirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
   Enzyme class 5: Chains A, B, C, D: E.C.3.6.1.15  - nucleoside-triphosphate phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + phosphate + H+
ribonucleoside 5'-triphosphate
+ H2O
= ribonucleoside 5'-diphosphate
+ phosphate
+ H(+)
Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
Proc Natl Acad Sci U S A 114:8017-8022 (2017)
PubMed id: 28696310  
 
 
Antibody-induced uncoating of human rhinovirus B14.
Y.Dong, Y.Liu, W.Jiang, T.J.Smith, Z.Xu, M.G.Rossmann.
 
  ABSTRACT  
 
Rhinoviruses (RVs) are the major causes of common colds in humans. They have a nonenveloped, icosahedral capsid surrounding a positive-strand RNA genome. Here we report that the antigen-binding (Fab) fragment of a neutralizing antibody (C5) can trigger genome release from RV-B14 to form emptied particles and neutralize virus infection. Using cryo-electron microscopy, structures of the C5 Fab in complex with the full and emptied particles have been determined at 2.3 Å and 3.0 Å resolution, respectively. Each of the 60 Fab molecules binds primarily to a region on viral protein 3 (VP3). Binding of the C5 Fabs to RV-B14 results in significant conformational changes around holes in the capsid through which the viral RNA might exit. These results are so far the highest resolution view of an antibody-virus complex and elucidate a mechanism whereby antibodies neutralize RVs and related viruses by inducing virus uncoating.
 

 

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