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Crystal structure of human adenovirus at 3.5 A resolution

Reddy, Vijay S ; Natchiar, S Kundhavai ; Stewart, Phoebe L ; Nemerow, Glen R

Science (New York, N.Y.), 27 August 2010, Vol.329(5995), pp.1071-5 [Tạp chí có phản biện]

E-ISSN: 1095-9203 ; PMID: 20798318 Version:1 ; DOI: 10.1126/science.1187292

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  • Nhan đề:
    Crystal structure of human adenovirus at 3.5 A resolution
  • Tác giả: Reddy, Vijay S ; Natchiar, S Kundhavai ; Stewart, Phoebe L ; Nemerow, Glen R
  • Chủ đề: Adenoviruses, Human -- Chemistry ; Capsid -- Chemistry ; Capsid Proteins -- Chemistry
  • Là 1 phần của: Science (New York, N.Y.), 27 August 2010, Vol.329(5995), pp.1071-5
  • Mô tả: Rational development of adenovirus vectors for therapeutic gene transfer is hampered by the lack of accurate structural information. Here, we report the x-ray structure at 3.5 angstrom resolution of the 150-megadalton adenovirus capsid containing nearly 1 million amino acids. We describe interactions between the major capsid protein (hexon) and several accessory molecules that stabilize the capsid. The virus structure also reveals an altered association between the penton base and the trimeric fiber protein, perhaps reflecting an early event in cell entry. The high-resolution structure provides a substantial advance toward understanding the assembly and cell entry mechanisms of a large double-stranded DNA virus and provides new opportunities for improving adenovirus-mediated gene transfer.
  • Ngôn ngữ: English
  • Số nhận dạng: E-ISSN: 1095-9203 ; PMID: 20798318 Version:1 ; DOI: 10.1126/science.1187292

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