4pt4: Difference between revisions
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pt4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pt4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pt4 RCSB], [http://www.ebi.ac.uk/pdbsum/4pt4 PDBsum]</span></td></tr> | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4pt4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4pt4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4pt4 RCSB], [http://www.ebi.ac.uk/pdbsum/4pt4 PDBsum]</span></td></tr> | ||
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== Publication Abstract from PubMed == | |||
The nucleoid-associated protein HU plays an important role in maintenance of chromosomal architecture and in global regulation of DNA transactions in bacteria. Although HU is essential for growth in Mycobacterium tuberculosis (Mtb), there have been no reported attempts to perturb HU function with small molecules. Here we report the crystal structure of the N-terminal domain of HU from Mtb. We identify a core region within the HU-DNA interface that can be targeted using stilbene derivatives. These small molecules specifically inhibit HU-DNA binding, disrupt nucleoid architecture and reduce Mtb growth. The stilbene inhibitors induce gene expression changes in Mtb that resemble those induced by HU deficiency. Our results indicate that HU is a potential target for the development of therapies against tuberculosis. | |||
Targeting Mycobacterium tuberculosis nucleoid-associated protein HU with structure-based inhibitors.,Bhowmick T, Ghosh S, Dixit K, Ganesan V, Ramagopal UA, Dey D, Sarma SP, Ramakumar S, Nagaraja V Nat Commun. 2014 Jun 11;5:4124. doi: 10.1038/ncomms5124. PMID:24916461<ref>PMID:24916461</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
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== References == | |||
<references/> | |||
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</StructureSection> | </StructureSection> | ||
Revision as of 09:01, 27 August 2014
Crystal structure Analysis of N terminal region containing the dimerization domain and DNA binding domain of HU protein(Histone like protein-DNA binding) from Mycobacterium tuberculosis [H37Rv]Crystal structure Analysis of N terminal region containing the dimerization domain and DNA binding domain of HU protein(Histone like protein-DNA binding) from Mycobacterium tuberculosis [H37Rv]
Structural highlights
Publication Abstract from PubMedThe nucleoid-associated protein HU plays an important role in maintenance of chromosomal architecture and in global regulation of DNA transactions in bacteria. Although HU is essential for growth in Mycobacterium tuberculosis (Mtb), there have been no reported attempts to perturb HU function with small molecules. Here we report the crystal structure of the N-terminal domain of HU from Mtb. We identify a core region within the HU-DNA interface that can be targeted using stilbene derivatives. These small molecules specifically inhibit HU-DNA binding, disrupt nucleoid architecture and reduce Mtb growth. The stilbene inhibitors induce gene expression changes in Mtb that resemble those induced by HU deficiency. Our results indicate that HU is a potential target for the development of therapies against tuberculosis. Targeting Mycobacterium tuberculosis nucleoid-associated protein HU with structure-based inhibitors.,Bhowmick T, Ghosh S, Dixit K, Ganesan V, Ramagopal UA, Dey D, Sarma SP, Ramakumar S, Nagaraja V Nat Commun. 2014 Jun 11;5:4124. doi: 10.1038/ncomms5124. PMID:24916461[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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