Seeing the Herpesvirus Capsid at 8.5 Å-Reference-Cited by-同舟云学术

Seeing the Herpesvirus Capsid at 8.5 Å

Published:2000-05-05 Issue:5467 Volume:288 Page:877-880
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Zhou Z. Hong¹,Dougherty Matthew²,Jakana Joanita²,He Jing³,Rixon Frazer J.⁴,Chiu Wah²³

Affiliation:

1. Department of Pathology and Laboratory Medicine, University of Texas–Houston Medical School, Houston, TX 77030, USA.

2. National Center for Macromolecular Imaging, Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX 77030, USA.

3. Graduate Program in Structural and Computational Biology and Molecular Biophysics, Baylor College of Medicine, Houston, TX 77030, USA.

4. MRC Virology Unit, Institute of Virology, Glasgow G11 5JR, Scotland, UK.

Abstract

Human herpesviruses are large and structurally complex viruses that cause a variety of diseases. The three-dimensional structure of the herpesvirus capsid has been determined at 8.5 angstrom resolution by electron cryomicroscopy. More than 30 putative α helices were identified in the four proteins that make up the 0.2 billion–dalton shell. Some of these helices are located at domains that undergo conformational changes during capsid assembly and DNA packaging. The unique spatial arrangement of the heterotrimer at the local threefold positions accounts for the asymmetric interactions with adjacent capsid components and the unusual co-dependent folding of its subunits.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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