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Crystal Structure of Human Adenovirus at 3.5 Å Resolution
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Crystal Structure of Human Adenovirus at 3.5 Å Resolution
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Crystal Structure of Human Adenovirus at 3.5 Å Resolution
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Journal Article
Crystal Structure of Human Adenovirus at 3.5 Å Resolution
2010
Overview
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.
Publisher
American Association for the Advancement of Science,The American Association for the Advancement of Science
Subject
/ Adenoviruses, Human - chemistry
/ Adenoviruses, Human - physiology
/ Adenoviruses, Human - ultrastructure
/ Biological and medical sciences
/ Capsid
/ Capsid Proteins - ultrastructure
/ Cements
/ DNA
/ Fundamental and applied biological sciences. Psychology
/ humans
/ Morphology, structure, chemical composition, physicochemical properties
/ Protein Interaction Domains and Motifs
/ Protein Structure, Secondary
/ Protein Subunits - chemistry
/ Proteins
/ Trimers
/ Virology
/ Viruses
