This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Love, R. A.
Right arrow Articles by Cronin, C. N.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Love, R. A.
Right arrow Articles by Cronin, C. N.

 Previous Article  |  Next Article 

Journal of Virology, May 2009, p. 4395-4403, Vol. 83, No. 9
0022-538X/09/$08.00+0     doi:10.1128/JVI.02352-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Crystal Structure of a Novel Dimeric Form of NS5A Domain I Protein from Hepatitis C Virus{triangledown}

Robert A. Love,* Oleg Brodsky, Michael J. Hickey, Peter A. Wells, and Ciarán N. Cronin

Structural Biology Group, Pfizer Global Research and Development, La Jolla Laboratories, San Diego, California 92121

Received 11 November 2008/ Accepted 13 February 2009

A new protein expression vector design utilizing an N-terminal six-histidine tag and tobacco etch virus protease cleavage site upstream of the hepatitis C virus NS5A sequence has resulted in a more straightforward purification method and improved yields of purified NS5A domain I protein. High-resolution diffracting crystals of NS5A domain I (amino acids 33 to 202) [NS5A(33-202)] were obtained by using detergent additive crystallization screens, leading to the structure of a homodimer which is organized differently from that published previously (T. L. Tellinghuisen, J. Marcotrigiano, and C. M. Rice, Nature 435:374-379, 2005) yet is consistent with a membrane association model for NS5A. The monomer-monomer interface of NS5A(33-202) features an extensive buried surface area involving the most-highly conserved face of each monomer. The two alternate structural forms of domain I now available may be indicative of the multiple roles emerging for NS5A in viral RNA replication and viral particle assembly.

* Corresponding author. Mailing address: 10777 Science Center Drive, San Diego, CA 92121. Phone: (858) 622-3022. Fax: (858) 678-8293. E-mail: robert.love{at}pfizer.com

{triangledown} Published ahead of print on 25 February 2009.

Journal of Virology, May 2009, p. 4395-4403, Vol. 83, No. 9
0022-538X/09/$08.00+0     doi:10.1128/JVI.02352-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»