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• W1972636859 endingPage "143" @default.
• W1972636859 startingPage "129" @default.
• W1972636859 abstract "Adenovirus and reovirus are nonenveloped viruses that engage cell-surface receptors using filamentous attachment proteins with head-and-tail morphology. The coxsackievirus and adenovirus receptor (CAR) and reovirus receptor junctional adhesion molecule 1 (JAM1) are immunoglobulin superfamily members that form homodimers stabilized by ionic and hydrophobic contacts between their N-terminal immunoglobulin-like domains. Both proteins are expressed at regions of cell-cell contact and contain sequences in their cytoplasmic tails that anchor the proteins to the actin cytoskeleton. Like CAR and JAM1, the attachment proteins of adenovirus and reovirus, fiber and σ1, respectively, also share key structural features. Both fiber and σ1 have defined regions of flexibility within the tail, which is constructed in part using an unusual triple β-spiral motif. The head domains of both proteins are formed by an 8-stranded β-barrel with identical β-strand connectivity. Strikingly, both adenovirus fiber and reovirus 1 engage their receptors by interacting with sequences that also mediate formation of receptor homodimers. Therefore, while adenovirus and reovirus belong to different virus families and have few overall properties in common, the observed similarities between the receptors and attachment proteins of these viruses suggest a conserved mechanism of attachment and an evolutionary relationship." @default.
• W1972636859 created "2016-06-24" @default.
• W1972636859 creator A5023812277 @default.
• W1972636859 creator A5029265500 @default.
• W1972636859 date "2004-06-01" @default.
• W1972636859 modified "2023-09-23" @default.
• W1972636859 title "Structural Similarities in the Cellular Receptors Used by Adenovirus and Reovirus" @default.
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• W1972636859 doi "https://doi.org/10.1089/0882824041310621" @default.
• W1972636859 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/15279694" @default.
• W1972636859 hasPublicationYear "2004" @default.
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