Crystal structure of human rhinovirus serotype 1A (HRV1A)

Sangsoo Kim, Thomas Smith, Michael S. Chapman, Michael G. Rossmann, Daniel C. Pevear, Frank J. Dutko, Peter J. Felock, Guy D. Diana, Mark A. McKinlay

Research output: Contribution to journalArticle

162 Citations (Scopus)

Abstract

The structure of human rhinovirus 1A (HRV1A) has been determined to 3.2 Å resolution using phase refinement and extension by symmetry averaging starting with phases at 5 Å resolution calculated from the known human rhinovirus 14 (HRV14) structure. The polypeptide backbone structures of HRV1A and HRV14 are similar, but the exposed surfaces are rather different. Differential charge distribution of amino acid residues in the "canyon", the putative receptor binding site, provides a possible explanation for the difference in minor versus major receptor group specificities, represented by HRV1A and HRV14, respectively. The hydrophobic pocket in VP1, into which antiviral compounds bind, is in an "open" conformation similar to that observed in drug-bound HRV14. Drug binding in HRV1A does not induce extensive conformational changes, in contrast to the case of HRV14.

Original languageEnglish (US)
Pages (from-to)91-111
Number of pages21
JournalJournal of Molecular Biology
Volume210
Issue number1
DOIs
StatePublished - Nov 5 1989
Externally publishedYes

Fingerprint

Rhinovirus
Serogroup
Pharmaceutical Preparations
Antiviral Agents
Binding Sites
Amino Acids
Peptides

ASJC Scopus subject areas

  • Virology

Cite this

Kim, S., Smith, T., Chapman, M. S., Rossmann, M. G., Pevear, D. C., Dutko, F. J., ... McKinlay, M. A. (1989). Crystal structure of human rhinovirus serotype 1A (HRV1A). Journal of Molecular Biology, 210(1), 91-111. https://doi.org/10.1016/0022-2836(89)90293-3

Crystal structure of human rhinovirus serotype 1A (HRV1A). / Kim, Sangsoo; Smith, Thomas; Chapman, Michael S.; Rossmann, Michael G.; Pevear, Daniel C.; Dutko, Frank J.; Felock, Peter J.; Diana, Guy D.; McKinlay, Mark A.

In: Journal of Molecular Biology, Vol. 210, No. 1, 05.11.1989, p. 91-111.

Research output: Contribution to journalArticle

Kim, S, Smith, T, Chapman, MS, Rossmann, MG, Pevear, DC, Dutko, FJ, Felock, PJ, Diana, GD & McKinlay, MA 1989, 'Crystal structure of human rhinovirus serotype 1A (HRV1A)', Journal of Molecular Biology, vol. 210, no. 1, pp. 91-111. https://doi.org/10.1016/0022-2836(89)90293-3
Kim, Sangsoo ; Smith, Thomas ; Chapman, Michael S. ; Rossmann, Michael G. ; Pevear, Daniel C. ; Dutko, Frank J. ; Felock, Peter J. ; Diana, Guy D. ; McKinlay, Mark A. / Crystal structure of human rhinovirus serotype 1A (HRV1A). In: Journal of Molecular Biology. 1989 ; Vol. 210, No. 1. pp. 91-111.
@article{b60fc86df106496493f197cb1e5b3b79,
title = "Crystal structure of human rhinovirus serotype 1A (HRV1A)",
abstract = "The structure of human rhinovirus 1A (HRV1A) has been determined to 3.2 {\AA} resolution using phase refinement and extension by symmetry averaging starting with phases at 5 {\AA} resolution calculated from the known human rhinovirus 14 (HRV14) structure. The polypeptide backbone structures of HRV1A and HRV14 are similar, but the exposed surfaces are rather different. Differential charge distribution of amino acid residues in the {"}canyon{"}, the putative receptor binding site, provides a possible explanation for the difference in minor versus major receptor group specificities, represented by HRV1A and HRV14, respectively. The hydrophobic pocket in VP1, into which antiviral compounds bind, is in an {"}open{"} conformation similar to that observed in drug-bound HRV14. Drug binding in HRV1A does not induce extensive conformational changes, in contrast to the case of HRV14.",
author = "Sangsoo Kim and Thomas Smith and Chapman, {Michael S.} and Rossmann, {Michael G.} and Pevear, {Daniel C.} and Dutko, {Frank J.} and Felock, {Peter J.} and Diana, {Guy D.} and McKinlay, {Mark A.}",
year = "1989",
month = "11",
day = "5",
doi = "10.1016/0022-2836(89)90293-3",
language = "English (US)",
volume = "210",
pages = "91--111",
journal = "Journal of Molecular Biology",
issn = "0022-2836",
publisher = "Academic Press Inc.",
number = "1",

}

TY - JOUR

T1 - Crystal structure of human rhinovirus serotype 1A (HRV1A)

AU - Kim, Sangsoo

AU - Smith, Thomas

AU - Chapman, Michael S.

AU - Rossmann, Michael G.

AU - Pevear, Daniel C.

AU - Dutko, Frank J.

AU - Felock, Peter J.

AU - Diana, Guy D.

AU - McKinlay, Mark A.

PY - 1989/11/5

Y1 - 1989/11/5

N2 - The structure of human rhinovirus 1A (HRV1A) has been determined to 3.2 Å resolution using phase refinement and extension by symmetry averaging starting with phases at 5 Å resolution calculated from the known human rhinovirus 14 (HRV14) structure. The polypeptide backbone structures of HRV1A and HRV14 are similar, but the exposed surfaces are rather different. Differential charge distribution of amino acid residues in the "canyon", the putative receptor binding site, provides a possible explanation for the difference in minor versus major receptor group specificities, represented by HRV1A and HRV14, respectively. The hydrophobic pocket in VP1, into which antiviral compounds bind, is in an "open" conformation similar to that observed in drug-bound HRV14. Drug binding in HRV1A does not induce extensive conformational changes, in contrast to the case of HRV14.

AB - The structure of human rhinovirus 1A (HRV1A) has been determined to 3.2 Å resolution using phase refinement and extension by symmetry averaging starting with phases at 5 Å resolution calculated from the known human rhinovirus 14 (HRV14) structure. The polypeptide backbone structures of HRV1A and HRV14 are similar, but the exposed surfaces are rather different. Differential charge distribution of amino acid residues in the "canyon", the putative receptor binding site, provides a possible explanation for the difference in minor versus major receptor group specificities, represented by HRV1A and HRV14, respectively. The hydrophobic pocket in VP1, into which antiviral compounds bind, is in an "open" conformation similar to that observed in drug-bound HRV14. Drug binding in HRV1A does not induce extensive conformational changes, in contrast to the case of HRV14.

UR - http://www.scopus.com/inward/record.url?scp=0024439180&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0024439180&partnerID=8YFLogxK

U2 - 10.1016/0022-2836(89)90293-3

DO - 10.1016/0022-2836(89)90293-3

M3 - Article

C2 - 2555523

AN - SCOPUS:0024439180

VL - 210

SP - 91

EP - 111

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

SN - 0022-2836

IS - 1

ER -