The structure of the human adenovirus 2 penton

被引:171
作者
Zubieta, C
Schoehn, G
Chroboczek, J
Cusack, S
机构
[1] European Mol Biol Lab, Grenoble Outstn, F-38042 Grenoble 9, France
[2] Inst Biol Struct JP Ebel, F-38027 Grenoble 1, France
[3] Univ Grenoble 1, Mol Virol Lab, EA 2939, Grenoble 9, France
关键词
D O I
10.1016/j.molcel.2004.11.041
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The adenovirus penton, a noncovalent complex of the pentameric penton base and trimeric fiber proteins, comprises the vertices of the adenovirus capsid and contains all necessary components for viral attachment and internalization. The 3.3 Angstrom resolution crystal structure of human adenovirus 2 (hAd2) penton base shows that the monomer has a basal jellyroll domain and a distal irregular domain formed by two long insertions, a similar topology to the adenovirus hexon. The Arg-Gly-Asp (RGD) motif, required for interactions with cellular integrins, occurs on a flexible surface loop. The complex of penton base with bound N-terminal fiber peptide, determined at 3.5 Angstrom resolution shows that the universal fiber motif FNPVYPY binds at the interface of adjacent penton base monomers and results in a localized structural rearrangement in the insertion domain of the penton base. These results give insight into the structure and assembly of the adenovirus capsid and will be of use for gene-therapy applications.
引用
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页码:121 / 135
页数:15
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