1jhi: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1jhi.gif|left|200px]] | [[Image:1jhi.gif|left|200px]] | ||
'''Solution Structure of a Hedamycin-DNA complex''' | {{Structure | ||
|PDB= 1jhi |SIZE=350|CAPTION= <scene name='initialview01'>1jhi</scene> | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=HEH:HEDAMYCIN'>HEH</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Solution Structure of a Hedamycin-DNA complex''' | |||
==Overview== | ==Overview== | ||
| Line 7: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
1JHI is a [ | 1JHI is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JHI OCA]. | ||
==Reference== | ==Reference== | ||
Structural investigation of the hedamycin:d(ACCGGT)2 complex by NMR and restrained molecular dynamics., Owen EA, Burley GA, Carver JA, Wickham G, Keniry MA, Biochem Biophys Res Commun. 2002 Feb 8;290(5):1602-8. PMID:[http:// | Structural investigation of the hedamycin:d(ACCGGT)2 complex by NMR and restrained molecular dynamics., Owen EA, Burley GA, Carver JA, Wickham G, Keniry MA, Biochem Biophys Res Commun. 2002 Feb 8;290(5):1602-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11820806 11820806] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Burley, G A.]] | [[Category: Burley, G A.]] | ||
| Line 21: | Line 30: | ||
[[Category: hedamycin]] | [[Category: hedamycin]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:03:29 2008'' | ||
Revision as of 10:03, 20 March 2008
| |||||||||||||
| 1jhi | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Ligands: | HEH | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Solution Structure of a Hedamycin-DNA complex
Overview
Hedamycin, a member of the pluramycin family of drugs, displays a range of biological responses including antitumor and antimicrobial activity. The mechanism of action is via direct interaction with DNA through intercalation between the bases of the oligonucleotide and alkylation of a guanine residue at 5'-PyG-3' sites. There appears to be some minor structural differences between two earlier studies on the interaction of hedamycin with 5'-PyG-3' sites. In this study, a high-resolution NMR analysis of the hedamycin:d(ACCGGT)2 complex was undertaken in order to investigate the effect of replacing the thymine with a guanine at the preferred 5'-CGT-3' site. The resultant structure was compared with earlier work, with particular emphasis placed on the drug conformation. The structure of the hedamycin:d(ACCGGT)2 complex has many features in common with the two previous NMR structures of hedamycin:DNA complexes but differed in the conformation and orientation of the N,N-dimethylvancosamine saccharide of hedamycin in one of these structures. The preferential binding of hedamycin to 5'-CG-3' over 5'-TG-3' binding sites is explained in terms of the orientation and location of the N,N-dimethylvancosamine saccharide in the minor groove.
About this Structure
1JHI is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
Structural investigation of the hedamycin:d(ACCGGT)2 complex by NMR and restrained molecular dynamics., Owen EA, Burley GA, Carver JA, Wickham G, Keniry MA, Biochem Biophys Res Commun. 2002 Feb 8;290(5):1602-8. PMID:11820806
Page seeded by OCA on Thu Mar 20 12:03:29 2008
