From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:2ew5.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:2ew5.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_2ew5| PDB=2ew5 | SCENE= }} | | {{STRUCTURE_2ew5| PDB=2ew5 | SCENE= }} |
| | | | |
| - | '''Structure of Helicobacter Pylori peptide deformylase in complex with inhibitor'''
| + | ===Structure of Helicobacter Pylori peptide deformylase in complex with inhibitor=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | Colonization of human stomach by the bacterium Helicobacter pylori is a major causative factor for gastrointestinal illnesses and gastric cancer. However, the discovery of anti-H. pylori agents is a difficult task due to lack of mature protein targets. Therefore, identifying new molecular targets for developing new drugs against H. pylori is obviously necessary. In this study, the in-house potential drug target database (PDTD, http://www.dddc.ac.cn/tarfisdock/) was searched by the reverse docking approach using an active natural product (compound 1) discovered by anti-H. pylori screening as a probe. Homology search revealed that, among the 15 candidates discovered by reverse docking, only diaminopimelate decarboxylase (DC) and peptide deformylase (PDF) have homologous proteins in the genome of H. pylori. Enzymatic assay demonstrated compound 1 and its derivative compound 2 are the potent inhibitors against H. pylori PDF (HpPDF) with IC50 values of 10.8 and 1.25 microM, respectively. X-ray crystal structures of HpPDF and the complexes of HpPDF with 1 and 2 were determined for the first time, indicating that these two inhibitors bind well with HpPDF binding pocket. All these results indicate that HpPDF is a potential target for screening new anti-H. pylori agents. In addition, compounds 1 and 2 were predicted to bind to HpPDF with relatively high selectivity, suggesting they can be used as leads for developing new anti-H. pylori agents. The results demonstrated that our strategy, reverse docking in conjunction with bioassay and structural biology, is effective and can be used as a complementary approach of functional genomics and chemical biology in target identification.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16882991}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16882991 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_16882991}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 26: |
Line 30: |
| | [[Category: Cobalt helicobacter pylori peptide deformylase]] | | [[Category: Cobalt helicobacter pylori peptide deformylase]] |
| | [[Category: Inhibitor]] | | [[Category: Inhibitor]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 03:10:58 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 03:39:35 2008'' |
Revision as of 00:39, 29 July 2008
Template:STRUCTURE 2ew5
Structure of Helicobacter Pylori peptide deformylase in complex with inhibitor
Template:ABSTRACT PUBMED 16882991
About this Structure
2EW5 is a Single protein structure of sequence from Helicobacter pylori. Full crystallographic information is available from OCA.
Reference
Peptide deformylase is a potential target for anti-Helicobacter pylori drugs: reverse docking, enzymatic assay, and X-ray crystallography validation., Cai J, Han C, Hu T, Zhang J, Wu D, Wang F, Liu Y, Ding J, Chen K, Yue J, Shen X, Jiang H, Protein Sci. 2006 Sep;15(9):2071-81. Epub 2006 Aug 1. PMID:16882991
Page seeded by OCA on Tue Jul 29 03:39:35 2008
