Human rhinovirus 14 complexed with antiviral compound R 61837

Michael S. Chapman; Iwona Minor; Michael G. Rossmann; Guy D. Diana; Koen Andries

doi:10.1016/0022-2836(91)90749-V

Human rhinovirus 14 complexed with antiviral compound R 61837

Michael S. Chapman, Iwona Minor, Michael G. Rossmann, Guy D. Diana, Koen Andries

Research output: Contribution to journal › Article › peer-review

48 Scopus citations

Abstract

The binding of the antirhinoviral agent R 61837 to human rhinovirus 14 has been examined by X-ray crystallographic methods. The compound R 61837 binds in the same pocket (underneath the canyon floor) as the "WIN" antirhinoviral agents. It does not penetrate as far into the pocket but causes similar conformational changes in the virus capsid. The movement of residues 1217 to 1221 of viral protein 1 (in the "FMDV loop") is more pronounced for R 61837 than for WIN compounds. Although both R 61837 and WIN antiviral agents partially fill the same hydrophobic pocket, atomic binding interactions differ, showing that considerable diversity in the nature of antiviral agents is possible.

Original language	English (US)
Pages (from-to)	455-463
Number of pages	9
Journal	Journal of molecular biology
Volume	217
Issue number	3
DOIs	https://doi.org/10.1016/0022-2836(91)90749-V
State	Published - Feb 5 1991
Externally published	Yes

ASJC Scopus subject areas

Structural Biology
Molecular Biology

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10.1016/0022-2836(91)90749-V

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@article{6a4730360873442a8c766edc28220a50,

title = "Human rhinovirus 14 complexed with antiviral compound R 61837",

abstract = "The binding of the antirhinoviral agent R 61837 to human rhinovirus 14 has been examined by X-ray crystallographic methods. The compound R 61837 binds in the same pocket (underneath the canyon floor) as the {"}WIN{"} antirhinoviral agents. It does not penetrate as far into the pocket but causes similar conformational changes in the virus capsid. The movement of residues 1217 to 1221 of viral protein 1 (in the {"}FMDV loop{"}) is more pronounced for R 61837 than for WIN compounds. Although both R 61837 and WIN antiviral agents partially fill the same hydrophobic pocket, atomic binding interactions differ, showing that considerable diversity in the nature of antiviral agents is possible.",

author = "Chapman, {Michael S.} and Iwona Minor and Rossmann, {Michael G.} and Diana, {Guy D.} and Koen Andries",

note = "Funding Information: Stanford Synchrotron Research Laboratory. We also thank Helene Prongay and Sharon Wilder for help in preparation of the manuscript. We gratefully acknowledge financial support from the National Science Foundation and the National Institutes of Health. The co-ordinates of the R 61837 complex with HRV14 are deposited with the Brookhaven Protein Data Bank.",

year = "1991",

month = feb,

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doi = "10.1016/0022-2836(91)90749-V",

language = "English (US)",

volume = "217",

pages = "455--463",

journal = "Journal of molecular biology",

issn = "0022-2836",

publisher = "Academic Press Inc.",

number = "3",

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TY - JOUR

T1 - Human rhinovirus 14 complexed with antiviral compound R 61837

AU - Chapman, Michael S.

AU - Minor, Iwona

AU - Rossmann, Michael G.

AU - Diana, Guy D.

AU - Andries, Koen

N1 - Funding Information: Stanford Synchrotron Research Laboratory. We also thank Helene Prongay and Sharon Wilder for help in preparation of the manuscript. We gratefully acknowledge financial support from the National Science Foundation and the National Institutes of Health. The co-ordinates of the R 61837 complex with HRV14 are deposited with the Brookhaven Protein Data Bank.

PY - 1991/2/5

Y1 - 1991/2/5

N2 - The binding of the antirhinoviral agent R 61837 to human rhinovirus 14 has been examined by X-ray crystallographic methods. The compound R 61837 binds in the same pocket (underneath the canyon floor) as the "WIN" antirhinoviral agents. It does not penetrate as far into the pocket but causes similar conformational changes in the virus capsid. The movement of residues 1217 to 1221 of viral protein 1 (in the "FMDV loop") is more pronounced for R 61837 than for WIN compounds. Although both R 61837 and WIN antiviral agents partially fill the same hydrophobic pocket, atomic binding interactions differ, showing that considerable diversity in the nature of antiviral agents is possible.

AB - The binding of the antirhinoviral agent R 61837 to human rhinovirus 14 has been examined by X-ray crystallographic methods. The compound R 61837 binds in the same pocket (underneath the canyon floor) as the "WIN" antirhinoviral agents. It does not penetrate as far into the pocket but causes similar conformational changes in the virus capsid. The movement of residues 1217 to 1221 of viral protein 1 (in the "FMDV loop") is more pronounced for R 61837 than for WIN compounds. Although both R 61837 and WIN antiviral agents partially fill the same hydrophobic pocket, atomic binding interactions differ, showing that considerable diversity in the nature of antiviral agents is possible.

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SP - 455

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JO - Journal of molecular biology

JF - Journal of molecular biology

IS - 3

ER -

Human rhinovirus 14 complexed with antiviral compound R 61837

Abstract

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