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5KEP

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

Summary for 5KEP
Entry DOI10.2210/pdb5kep/pdb
Related5KEQ 5KEY 5KGB
EMDB information6619 6620 8243
DescriptorMajor capsid protein L1 (1 entity in total)
Functional Keywordshpv16, l1 protein, asymmetric unit, virus like particle
Biological sourceHuman papillomavirus type 16
Cellular locationVirion : P03101
Total number of polymer chains6
Total formula weight323652.65
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 citationGuan, 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: 28065506
DOI: 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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건을2025-04-23부터공개중

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