2C6S

human adenovirus penton base 2 12 chimera

2C6S の概要

• エントリーDOI: 10.2210/pdb2c6s/pdb
• 関連するPDBエントリー: 1X9P 1X9T 2BLD 2BVI
• 分子名称: ADENOVIRUS 2,12 PENTON BASE CHIMERA (1 entity in total)
• 機能のキーワード: virus/viral protein, adenovirus, capsid, penton, dodecahedra, fiber, viral protein, virus-viral protein complex
• 由来する生物種: HUMAN ADENOVIRUS C
• タンパク質・核酸の鎖数: 15
• 化学式量合計: 873039.90

構造登録者

Zubieta, C.,Blanchoin, L.,Cusack, S. (登録日: 2005-11-11, 公開日: 2006-09-06, 最終更新日: 2023-12-13)

主引用文献

Zubieta, C.,Blanchoin, L.,Cusack, S.
Structural and Biochemical Characterization of a Human Adenovirus 2/12 Penton Base Chimera.
FEBS J., 273:4336-, 2006

PubMed Abstract: The vertex of the adenoviral capsid is formed by the penton, a complex of two proteins, the pentameric penton base and the trimeric fiber protein. The penton contains all necessary components for viral attachment and entry into the host cell. After initial attachment via the head domain of the fiber protein, the penton base interacts with cellular integrins through an Arg-Gly-Asp (RGD) motif located in a hypervariable surface loop, triggering virus internalization. In order to investigate the structural and functional role of this region, we replaced the hypervariable loop of serotype 2 with the corresponding, but much shorter, loop of serotype 12 and compared it to the wild type. Here, we report the 3.6 A crystal structure of a human adenovirus 2/12 penton base chimera crystallized as a dodecamer. The structure is generally similar to human adenovirus 2 penton base, with the main differences localized to the fiber protein-binding site. Fluorescence anisotropy assays using a trimeric fiber protein mimetic called the minifiber and wild-type human adenovirus 2 and chimeric penton base demonstrate that fiber protein binding is independent of the hypervariable loop, with a K(d) for fiber binding estimated in the 1-2 microm range. Interestingly, competition assays using labeled and unlabeled minifiber demonstrated virtually irreversible binding to the penton base, which we ascribe to a conformational change, on the basis of comparisons of all available penton base structures.

PubMed: 16939624
DOI: 10.1111/J.1742-4658.2006.05430.X

実験手法

X-RAY DIFFRACTION (3.6 Å)