The SV40 capsid is stabilized by a conserved pentapeptide hinge of the major capsid protein VP1.

ABSTRACT: The simian virus 40 (SV40) outer shell is composed of 72 pentamers of VP1. The core of the VP1 monomer is a beta-barrel with jelly-roll topology and extending N- and C-terminal arms. A pentapeptide hinge, KNPYP, tethers the C-arm to the VP1 beta-barrel core. The five C-arms that extend from each pentamer insert into the neighbouring pentamers, tying them together through different types of interactions. In the mature virion, this element adopts either of six conformations according to their location in the capsid. We found that the hinge is conserved among 16 members of the Polyomaviridae, attesting to its importance in capsid assembly and/or structure. We have used site-directed mutagenesis to gain an understanding into the structural requirements of this element: Y299 was changed to A, F

SUBMITTER: Ben-nun-Shaul O 

PROVIDER: S-EPMC2718546 | biostudies-literature | 2009 Mar

REPOSITORIES: biostudies-literature