5KEQ

High resolution cryo-EM maps of Human papillomavirus 16 reveal L2 location and heparin-induced conformational changes


Experimental Data Snapshot

  • Method: ELECTRON MICROSCOPY
  • Resolution: 4.30 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

wwPDB Validation   3D Report Full Report


This is version 1.4 of the entry. See complete history


Literature

Cryoelectron Microscopy Maps of Human Papillomavirus 16 Reveal L2 Densities and Heparin Binding Site.

Guan, J.Bywaters, S.M.Brendle, S.A.Ashley, R.E.Makhov, A.M.Conway, J.F.Christensen, N.D.Hafenstein, S.

(2017) Structure 25: 253-263

  • DOI: https://doi.org/10.1016/j.str.2016.12.001
  • Primary Citation of Related Structures:  
    5KEP, 5KEQ

  • PubMed Abstract: 

    Human papillomavirus (HPV) is a significant health burden and leading cause of virus-induced cancers. The current commercial vaccines are genotype specific and provide little therapeutic benefit to patients with existing HPV infections. Host entry mechanisms represent an excellent target for alternative therapeutics, but HPV receptor use, the details of cell attachment, and host entry are inadequately understood. Here we present near-atomic resolution structures of the HPV16 capsid and HPV16 in complex with heparin, both determined from cryoelectron micrographs collected with direct electron detection technology. The structures clarify details of capsid architecture for the first time, including variation in L1 major capsid protein conformation and putative location of L2 minor protein. Heparin binds specifically around the capsid icosahedral vertices and may recapitulate the earliest stage of infection, providing a framework for continuing biochemical, genetic, and biophysical studies.


  • Organizational Affiliation

    Division of Infectious Diseases, Department of Medicine, Penn State College of Medicine, The Pennsylvania State University College of Medicine, Mail Code H036, 500 University Drive, P.O. Box 850, Hershey, PA 17033-0850, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Major capsid protein L1
A, B, C, D, E
A, B, C, D, E, F
483Human papillomavirus 16Mutation(s): 0 
Gene Names: L1
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: ELECTRON MICROSCOPY
  • Resolution: 4.30 Å
  • Aggregation State: PARTICLE 
  • Reconstruction Method: SINGLE PARTICLE 

Structure Validation

View Full Validation Report



Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
National Institutes of Health/Office of the DirectorUnited StatesS10OD019995
National Institutes of Health/Office of the DirectorUnited StatesS10OD011986

Revision History  (Full details and data files)

  • Version 1.0: 2017-01-25
    Type: Initial release
  • Version 1.1: 2017-02-22
    Changes: Database references
  • Version 1.2: 2017-09-13
    Changes: Author supporting evidence, Data collection
  • Version 1.3: 2017-12-06
    Changes: Database references
  • Version 1.4: 2023-04-05
    Changes: Database references, Derived calculations