1DZL

L1 protein of human papillomavirus 16


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.50 Å
  • R-Value Free: 0.290 
  • R-Value Work: 0.280 
  • R-Value Observed: 0.280 

wwPDB Validation   3D Report Full Report


This is version 1.2 of the entry. See complete history


Literature

Structure of Small Virus-Like Particles Assembled from the L1 Protein of Human Papillomavirus 16

Chen, X.J.Garcea, B.Goldberg, I.Casini, G.Harrison, S.C.

(2000) Mol Cell 5: 557

  • DOI: https://doi.org/10.1016/s1097-2765(00)80449-9
  • Primary Citation of Related Structures:  
    1DZL

  • PubMed Abstract: 

    The papillomavirus major late protein, L1, forms the pentameric assembly unit of the viral shell. Recombinant HPV16 L1 pentamers assemble in vitro into capsid-like structures, and truncation of ten N-terminal residues leads to a homogeneous preparation of 12-pentamer, icosahedral particles. X-ray crystallographic analysis of these particles at 3.5 A resolution shows that L1 closely resembles VP1 from polyomaviruses. Surface loops contain the sites of sequence variation among HPV types and the locations of dominant neutralizing epitopes. The ease with which small virus-like particles may be obtained from L1 expressed in E. coli makes them attractive candidate components of a papillomavirus vaccine. Their crystal structure also provides a starting point for future vaccine design.


  • Organizational Affiliation

    Department of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts 02138, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
LATE MAJOR CAPSID PROTEIN L1505Human papillomavirus 16Mutation(s): 1 
UniProt
Find proteins for P03101 (Human papillomavirus type 16)
Explore P03101 
Go to UniProtKB:  P03101
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP03101
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.50 Å
  • R-Value Free: 0.290 
  • R-Value Work: 0.280 
  • R-Value Observed: 0.280 
  • Space Group: P 21 3
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 387α = 90
b = 387β = 90
c = 387γ = 90
Software Package:
Software NamePurpose
X-PLORrefinement
X-PLORphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2000-03-09
    Type: Initial release
  • Version 1.1: 2011-05-07
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance