Title |
Crystal structure of a new benzoic acid inhibitor of influenza neuraminidase bound with a new tilt induced by overpacking subsite C6
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Published in |
BMC Molecular and Cell Biology, May 2012
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DOI | 10.1186/1472-6807-12-7 |
Pubmed ID | |
Authors |
Lalitha Venkatramani, Eric S Johnson, Gundurao Kolavi, Gillian M Air, Wayne J Brouillette, Blaine HM Mooers |
Abstract |
Influenza neuraminidase (NA) is an important target for antiviral inhibitors since its active site is highly conserved such that inhibitors can be cross-reactive against multiple types and subtypes of influenza. Here, we discuss the crystal structure of neuraminidase subtype N9 complexed with a new benzoic acid based inhibitor (2) that was designed to add contacts by overpacking one side of the active site pocket. Inhibitor 2 uses benzoic acid to mimic the pyranose ring, a bis-(hydroxymethyl)-substituted 2-pyrrolidinone ring in place of the N-acetyl group of the sialic acid, and a branched aliphatic structure to fill the sialic acid C6 subsite. |
X Demographics
Geographical breakdown
Country | Count | As % |
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Unknown | 1 | 100% |
Demographic breakdown
Type | Count | As % |
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Practitioners (doctors, other healthcare professionals) | 1 | 100% |
Mendeley readers
Geographical breakdown
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India | 1 | 7% |
Unknown | 14 | 93% |
Demographic breakdown
Readers by professional status | Count | As % |
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Researcher | 4 | 27% |
Student > Bachelor | 2 | 13% |
Student > Ph. D. Student | 2 | 13% |
Student > Postgraduate | 2 | 13% |
Professor > Associate Professor | 2 | 13% |
Other | 2 | 13% |
Unknown | 1 | 7% |
Readers by discipline | Count | As % |
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Biochemistry, Genetics and Molecular Biology | 3 | 20% |
Chemistry | 3 | 20% |
Agricultural and Biological Sciences | 3 | 20% |
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Business, Management and Accounting | 1 | 7% |
Other | 2 | 13% |
Unknown | 2 | 13% |