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5W1O

Crystal Structure of HPV16 L1 Pentamer Bound to Heparin Oligosaccharides

Replaces:  3OAE
Summary for 5W1O
Entry DOI10.2210/pdb5w1o/pdb
DescriptorMajor capsid protein L1, 2-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-alpha-D-glucopyranose, 2-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-alpha-D-glucopyranose, ... (4 entities in total)
Functional Keywordshuman papillomavirus, jelly roll, capsid protein, receptor hspg, virus capsid, viral protein
Biological sourceHuman papillomavirus
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Total number of polymer chains5
Total formula weight244217.01
Authors
Dasgupta, J.,Chen, X.S. (deposition date: 2017-06-04, release date: 2017-10-18, Last modification date: 2023-10-04)
Primary citationDasgupta, J.,Bienkowska-Haba, M.,Ortega, M.E.,Patel, H.D.,Bodevin, S.,Spillmann, D.,Bishop, B.,Sapp, M.,Chen, X.S.
Structural basis of oligosaccharide receptor recognition by human papillomavirus.
J. Biol. Chem., 286:2617-2624, 2011
Cited by
PubMed Abstract: High risk human papillomavirus types 16 (HPV16) and 18 (HPV18) can cause cervical cancer. Efficient infection by HPV16 and HPV18 pseudovirions requires interactions of particles with cell-surface receptor heparan sulfate oligosaccharide. To understand the virus-receptor interactions for HPV infection, we determined the crystal structures of HPV16 and HPV18 capsids bound to the oligosaccharide receptor fragment using oligomeric heparin. The HPV-heparin structures revealed multiple binding sites for the highly negatively charged oligosaccharide fragment on the capsid surface, which is different from previously reported virus-receptor interactions in which a single type of binding pocket is present for a particular receptor. We performed structure-guided mutagenesis to generate mutant viruses, and cell binding and infectivity assays demonstrated the functional role of viral residues involved in heparin binding. These results provide a basis for understanding virus-heparan sulfate receptor interactions critical for HPV infection and for the potential development of inhibitors against HPV infection.
PubMed: 21115492
DOI: 10.1074/jbc.M110.160184
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.8 Å)
Structure validation

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