Submit Papers Directly to PNAS via Track II Sign up for PNAS Online eTocs
Link: Info for AuthorsLink: Editorial BoardLink: AboutLink: SubscribeLink: AdvertiseLink: ContactLink: Sitemap Link: PNAS Home
Proceedings of the National Academy of Sciences
Link: Current Issue "" Link: Archives "" Link: Online Submission ""  Link: Advanced Search



This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a colleague
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 Add to My File Cabinet
Right arrow Download to citation manager
Right arrow Request Copyright Permission
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Badger, J.
Right arrow Articles by Heinz, B. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Badger, J.
Right arrow Articles by Heinz, B. A.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg  
What's this?

 Previous Article  | Table of Contents |  Next Article 

PNAS | May 15, 1988 | vol. 85 | no. 10 | 3304-3308
Copyright © 1988 by the National Academy of Sciences

Structural Analysis of a Series of Antiviral Agents Complexed with Human Rhinovirus 14

John Badger, Iwona Minor, Marcia J. Kremer, Marcos A. Oliveira, Thomas J. Smith, James P. Griffith, Diego M. A. Guerin, S. Krishnaswamy, Ming Luo, Michael G. Rossmann, Mark A. McKinlay, Guy D. Diana, Frank J. Dutko, Marilyn Fancher, Roland R. Rueckert, and Beverly A. Heinz

The binding to human rhinovirus 14 of a series of eight antiviral agents that inhibit picornaviral uncoating after entry into host cells has been characterized crystallographically. All of these bind into the same hydrophobic pocket within the viral protein VP1 ß -barrel structure, although the orientation and position of each compound within the pocket was found to differ. The compounds cause the protein shell to be less flexible, thereby inhibiting disassembly. Although the antiviral potency of these compounds varies by 120-fold, they all induce the same conformational changes on the virion. The interactions of these compounds with the viral capsid are consistent with their observed antiviral activities against human rhinovirus 14 drug-resistant mutants and other rhinovirus serotypes. Crystallographic studies of one of these mutants confirm the partial sequencing data and support the finding that this is a single mutation that occurs within the binding pocket.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg    What's this?


This article has been cited by other articles in HighWire Press-hosted journals:


Home page
 Protein Sci.Home page
L. Wang and D. L. Smith
Capsid structure and dynamics of a human rhinovirus probed by hydrogen exchange mass spectrometry
Protein Sci., June 1, 2005; 14(6): 1661 - 1672.
[Abstract] [Full Text] [PDF]

Home page
 J. Virol.Home page
Y. Zhang, A. A. Simpson, R. M. Ledford, C. M. Bator, S. Chakravarty, G. A. Skochko, T. M. Demenczuk, A. Watanyar, D. C. Pevear, and M. G. Rossmann
Structural and Virological Studies of the Stages of Virus Replication That Are Affected by Antirhinovirus Compounds
J. Virol., October 15, 2004; 78(20): 11061 - 11069.
[Abstract] [Full Text] [PDF]

Home page
 J. Virol.Home page
D. Melamed, M. Mark-Danieli, M. Kenan-Eichler, O. Kraus, A. Castiel, N. Laham, T. Pupko, F. Glaser, N. Ben-Tal, and E. Bacharach
The Conserved Carboxy Terminus of the Capsid Domain of Human Immunodeficiency Virus Type 1 Gag Protein Is Important for Virion Assembly and Release
J. Virol., September 15, 2004; 78(18): 9675 - 9688.
[Abstract] [Full Text] [PDF]

Home page
 J. Virol.Home page
C. Xiao, T. J. Tuthill, C. M. Bator Kelly, L. J. Challinor, P. R. Chipman, R. A. Killington, D. J. Rowlands, A. Craig, and M. G. Rossmann
Discrimination among Rhinovirus Serotypes for a Variant ICAM-1 Receptor Molecule
J. Virol., September 15, 2004; 78(18): 10034 - 10044.
[Abstract] [Full Text] [PDF]

Home page
 Antimicrob. Agents Chemother.Home page
S. Hoglund, J. Su, S. S. Reneby, A. Vegvari, S. Hjerten, I.-M. Sintorn, H. Foster, Y.-P. Wu, I. Nystrom, and A. Vahlne
Tripeptide Interference with Human Immunodeficiency Virus Type 1 Morphogenesis
Antimicrob. Agents Chemother., November 1, 2002; 46(11): 3597 - 3605.
[Abstract] [Full Text] [PDF]

Home page
 Protein Sci.Home page
L. Wang, L. C. Lane, and D. L. Smith
Detecting structural changes in viral capsids by hydrogen exchange and mass spectrometry
Protein Sci., June 1, 2001; 10(6): 1234 - 1243.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
A. T. Hadfield, G. D. Diana, and M. G. Rossmann
Analysis of three structurally related antiviral compounds in complex with human rhinovirus 16
PNAS, December 21, 1999; 96(26): 14730 - 14735.
[Abstract] [Full Text] [PDF]

Home page
 Antimicrob. Agents Chemother.Home page
D. C. Pevear, T. M. Tull, M. E. Seipel, and J. M. Groarke
Activity of Pleconaril against Enteroviruses
Antimicrob. Agents Chemother., September 1, 1999; 43(9): 2109 - 2115.
[Abstract] [Full Text]

Home page
 Proc. Natl. Acad. Sci. USAHome page
N. Vaidehi and W. A. Goddard III
The pentamer channel stiffening model for drug action on human rhinovirus HRV-1A
PNAS, March 18, 1997; 94(6): 2466 - 2471.
[Abstract] [Full Text] [PDF]

Home page
 CirculationHome page
J. Fohlman, K. Pauksen, T. Hyypia, G. Eggertsen, A. Ehrnst, N.G. Ilback, and G. Friman
Antiviral Treatment With WIN 54 954 Reduces Mortality in Murine Coxsackievirus B3 Myocarditis
Circulation, November 1, 1996; 94(9): 2254 - 2259.
[Abstract] [Full Text]