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The quasi-atomic model of Human Adenovirus type 5 capsidThe quasi-atomic model of Human Adenovirus type 5 capsid
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Structural highlights
FunctionCAPSH_ADE05 Major capsid protein that self-associates to form 240 hexon trimers, each in the shape of a hexagon, building most of the pseudo T=25 capsid. Assembled into trimeric units with the help of the chaperone shutoff protein (By similarity). Transported by pre-protein VI to the nucleus where it associates with other structural proteins to form an empty capsid. Might be involved, through its interaction with host dyneins, in the intracellular microtubule-dependent transport of incoming viral capsid to the nucleus. Publication Abstract from PubMedAdenoviruses infect a wide range of vertebrates including humans. Their icosahedral capsids are composed of three major proteins: the trimeric hexon forms the facets and the penton, a noncovalent complex of the pentameric penton base and trimeric fibre proteins, is located at the 12 capsid vertices. Several proteins (IIIa, VI, VIII and IX) stabilise the capsid. We have obtained a 10 A resolution map of the human adenovirus 5 by image analysis from cryo-electron micrographs (cryoEMs). This map, in combination with the X-ray structures of the penton base and hexon, was used to build a quasi-atomic model of the arrangement of the two major capsid components and to analyse the hexon-hexon and hexon-penton interactions. The secondary proteins, notably VIII, were located by comparing cryoEM maps of native and pIX deletion mutant virions. Minor proteins IX and IIIa are located on the outside of the capsid, whereas protein VIII is organised with a T=2 lattice on the inner face of the capsid. The capsid organisation is compared with the known X-ray structure of bacteriophage PRD1. A quasi-atomic model of human adenovirus type 5 capsid.,Fabry CM, Rosa-Calatrava M, Conway JF, Zubieta C, Cusack S, Ruigrok RW, Schoehn G EMBO J. 2005 May 4;24(9):1645-54. Epub 2005 Apr 21. PMID:15861131[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |