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Conformational Changes of the Flavivirus E Glycoprotein

Zhang, Ying and Zhang, Wei and Ogata, Steven and Clements, David and Strauss, James H. and Baker, Timothy S. and Kuhn, Richard J. and Rossmann, Michael G. (2004) Conformational Changes of the Flavivirus E Glycoprotein. Structure, 12 (9). pp. 1607-1618. ISSN 09692126. PMCID PMC4152830. https://resolver.caltech.edu/CaltechAUTHORS:20160111-150851804

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Abstract

Dengue virus, a member of the Flaviviridae family, has a surface composed of 180 copies each of the envelope (E) glycoprotein and the membrane (M) protein. The crystal structure of an N-terminal fragment of E has been determined and compared with a previously described structure. The primary difference between these structures is a 10° rotation about a hinge relating the fusion domain DII to domains DI and DIII. These two rigid body components were used for independent fitting of E into the cryo-electron microscopy maps of both immature and mature dengue viruses. The fitted E structures in these two particles showed a difference of 27° between the two components. Comparison of the E structure in its postfusion state with that in the immature and mature virions shows a rotation approximately around the same hinge. Flexibility of E is apparently a functional requirement for assembly and infection of flaviviruses.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1016/j.str.2004.06.019DOIArticle
http://www.sciencedirect.com/science/article/pii/S0969212604002722PublisherArticle
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4152830/PubMed CentralArticle
Additional Information:© 2004 Elsevier Ltd. Received: April 22, 2004. Revised: June 29, 2004. Accepted: June 29, 2004. Published: September 7, 2004. We thank Suchetana (Tuli) Mukhopadhyay for many helpful discussions, as well as Sharon Wilder and Cheryl Towell for the preparation of the manuscript. We are grateful to Narayanasamy Nandhagopal and Alan A. Simpson, as well as people working at APS BioCARS, for help in data collection. The work was supported by NIH Program Project grants to R.J.K., M.G.R., and T.S.B. (AI 55672, AI 45976). Accession Numbers: Coordinates of the DEN sE(P) crystal structure and the fitted sE structures in both mature and immature virions have been deposited with the PDB (accession numbers are 1TG8, 1THD, and 1TGE, respectively).
Funders:
Funding AgencyGrant Number
NIHAI 55672
NIHAI 45976
Issue or Number:9
PubMed Central ID:PMC4152830
Record Number:CaltechAUTHORS:20160111-150851804
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20160111-150851804
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:63552
Collection:CaltechAUTHORS
Deposited By: Donna Wrublewski
Deposited On:12 Jan 2016 23:17
Last Modified:03 Oct 2019 09:29

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