Crystal Structures of the PBP2 Glycosyltransferase Domain: New Opportunities for Antibacterial Drug Design
The recent publication by Strynadka and colleagues, describing the first X‐ray structures of a soluble truncated version of PBP2 containing both glycosyltransferase and transpeptidase domains facilitates more common and feasible approaches for the rational design and in turn clinically useful GT‐inh...
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| Veröffentlicht in: | ChemMedChem 2007-10, Vol.2 (10), p.1403-1404 |
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| creator | Zuegg, Johannes Meutermans, Wim |
| description | The recent publication by Strynadka and colleagues, describing the first X‐ray structures of a soluble truncated version of PBP2 containing both glycosyltransferase and transpeptidase domains facilitates more common and feasible approaches for the rational design and in turn clinically useful GT‐inhibitors for the treatment of infections caused by highly resistant bacterial organisms. |
| doi_str_mv | 10.1002/cmdc.200700114 |
| format | Article |
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| language | eng |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete |
| subjects | Anti-Bacterial Agents - chemistry antibacterials Binding Sites Crystallography, X-Ray Drug Design glycosyltransferase Glycosyltransferases - antagonists & inhibitors Glycosyltransferases - chemistry Models, Molecular Oligosaccharides - chemistry Oligosaccharides - pharmacology peptidoglycan Protein Conformation transpeptidase |
| title | Crystal Structures of the PBP2 Glycosyltransferase Domain: New Opportunities for Antibacterial Drug Design |
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