File Download
There are no files associated with this item.
Links for fulltext
(May Require Subscription)
- Publisher Website: 10.1016/j.chembiol.2007.12.013
- Scopus: eid_2-s2.0-39149144502
- PMID: 18291323
- WOS: WOS:000253671000015
- Find via
Supplementary
- Citations:
- Appears in Collections:
Article: Probing FtsZ and Tubulin with C8-Substituted GTP Analogs Reveals Differences in Their Nucleotide Binding Sites
Title | Probing FtsZ and Tubulin with C8-Substituted GTP Analogs Reveals Differences in Their Nucleotide Binding Sites |
---|---|
Authors | |
Keywords | CHEMBIO CELLBIO |
Issue Date | 2008 |
Citation | Chemistry and Biology, 2008, v. 15, n. 2, p. 189-199 How to Cite? |
Abstract | The cytoskeletal proteins, FtsZ and tubulin, play a pivotal role in prokaryotic cell division and eukaryotic chromosome segregation, respectively. Selective inhibitors of the GTP-dependent polymerization of FtsZ could constitute a new class of antibiotics, while several inhibitors of tubulin are widely used in antiproliferative therapy. In this work, we set out to identify selective inhibitors of FtsZ based on the structure of its natural ligand, GTP. We found that GTP analogs with small hydrophobic substituents at C8 of the nucleobase efficiently inhibit FtsZ polymerization, whereas they have an opposite effect on the polymerization of tubulin. The inhibitory activity of the GTP analogs on FtsZ polymerization allowed us to crystallize FtsZ in complex with C8-morpholino-GTP, revealing the binding mode of a GTP derivative containing a nonmodified triphosphate chain. © 2008 Elsevier Ltd. All rights reserved. |
Persistent Identifier | http://hdl.handle.net/10722/219561 |
ISSN | 2017 Impact Factor: 5.915 |
ISI Accession Number ID |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Läppchen, Tilman | - |
dc.contributor.author | Pinas, Victorine A. | - |
dc.contributor.author | Hartog, Aloysius F. | - |
dc.contributor.author | Koomen, Gerrit Jan | - |
dc.contributor.author | Schaffner-Barbero, Claudia | - |
dc.contributor.author | Andreu, José Manuel | - |
dc.contributor.author | Trambaiolo, Daniel | - |
dc.contributor.author | Löwe, Jan | - |
dc.contributor.author | Juhem, Aurélie | - |
dc.contributor.author | Popov, Andrei V. | - |
dc.contributor.author | den Blaauwen, Tanneke | - |
dc.date.accessioned | 2015-09-23T02:57:24Z | - |
dc.date.available | 2015-09-23T02:57:24Z | - |
dc.date.issued | 2008 | - |
dc.identifier.citation | Chemistry and Biology, 2008, v. 15, n. 2, p. 189-199 | - |
dc.identifier.issn | 1074-5521 | - |
dc.identifier.uri | http://hdl.handle.net/10722/219561 | - |
dc.description.abstract | The cytoskeletal proteins, FtsZ and tubulin, play a pivotal role in prokaryotic cell division and eukaryotic chromosome segregation, respectively. Selective inhibitors of the GTP-dependent polymerization of FtsZ could constitute a new class of antibiotics, while several inhibitors of tubulin are widely used in antiproliferative therapy. In this work, we set out to identify selective inhibitors of FtsZ based on the structure of its natural ligand, GTP. We found that GTP analogs with small hydrophobic substituents at C8 of the nucleobase efficiently inhibit FtsZ polymerization, whereas they have an opposite effect on the polymerization of tubulin. The inhibitory activity of the GTP analogs on FtsZ polymerization allowed us to crystallize FtsZ in complex with C8-morpholino-GTP, revealing the binding mode of a GTP derivative containing a nonmodified triphosphate chain. © 2008 Elsevier Ltd. All rights reserved. | - |
dc.language | eng | - |
dc.relation.ispartof | Chemistry and Biology | - |
dc.subject | CHEMBIO | - |
dc.subject | CELLBIO | - |
dc.title | Probing FtsZ and Tubulin with C8-Substituted GTP Analogs Reveals Differences in Their Nucleotide Binding Sites | - |
dc.type | Article | - |
dc.description.nature | link_to_OA_fulltext | - |
dc.identifier.doi | 10.1016/j.chembiol.2007.12.013 | - |
dc.identifier.pmid | 18291323 | - |
dc.identifier.scopus | eid_2-s2.0-39149144502 | - |
dc.identifier.volume | 15 | - |
dc.identifier.issue | 2 | - |
dc.identifier.spage | 189 | - |
dc.identifier.epage | 199 | - |
dc.identifier.isi | WOS:000253671000015 | - |
dc.identifier.issnl | 1074-5521 | - |