5KEP
High resolution cryo-EM maps of Human Papillomavirus 16 reveal L2 location and heparin-induced conformational changes
Summary for 5KEP
Entry DOI | 10.2210/pdb5kep/pdb |
Related | 5KEQ 5KEY 5KGB |
EMDB information | 6619 6620 8243 |
Descriptor | Major capsid protein L1 (1 entity in total) |
Functional Keywords | hpv16, l1 protein, asymmetric unit, virus like particle |
Biological source | Human papillomavirus type 16 |
Cellular location | Virion : P03101 |
Total number of polymer chains | 6 |
Total formula weight | 323652.65 |
Authors | Guan, J.,Bywaters, S.M.,Brendle, S.A.,Ashley, R.E.,Makhov, A.M.,Conway, J.F.,Christensen, N.D.,Hafenstein, S. (deposition date: 2016-06-10, release date: 2017-01-25, Last modification date: 2024-05-15) |
Primary citation | Guan, J.,Bywaters, S.M.,Brendle, S.A.,Ashley, R.E.,Makhov, A.M.,Conway, J.F.,Christensen, N.D.,Hafenstein, S. Cryoelectron Microscopy Maps of Human Papillomavirus 16 Reveal L2 Densities and Heparin Binding Site. Structure, 25:253-263, 2017 Cited by 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. PubMed: 28065506DOI: 10.1016/j.str.2016.12.001 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (4.3 Å) |
Structure validation
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