Roles for human papillomavirus type 16 l1 cysteine residues 161, 229, and 379 in genome encapsidation and capsid stability.
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ABSTRACT:
SUBMITTER: Ryndock EJ
PROVIDER: S-EPMC4053435 | biostudies-literature | 2014
REPOSITORIES: biostudies-literature
Publications
Roles for human papillomavirus type 16 l1 cysteine residues 161, 229, and 379 in genome encapsidation and capsid stability.
Ryndock Eric J EJ Conway Michael J MJ Alam Samina S Gul Sana S Murad Sheeba S Christensen Neil D ND Meyers Craig C
PloS one 20140611 6
Human papillomavirus (HPV) capsids are formed through a network of inter- and intra-pentameric hydrophobic interactions and disulfide bonds. 72 pentamers of the major capsid protein, L1, and an unknown amount of the minor capsid protein, L2, form the structure of the capsid. There are 12 conserved L1 cysteine residues in HPV16. While C175, C185, and C428 have been implicated in the formation of a critical inter-pentameric disulfide bond, no structural or functional roles have been firmly attribu ...[more]
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