2oqs: Difference between revisions
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'''Structure of the hDLG/SAP97 PDZ2 in complex with HPV-18 papillomavirus E6 peptide''' | {{Structure | ||
|PDB= 2oqs |SIZE=350|CAPTION= <scene name='initialview01'>2oqs</scene> | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= DLG1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''Structure of the hDLG/SAP97 PDZ2 in complex with HPV-18 papillomavirus E6 peptide''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2OQS is a [ | 2OQS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OQS OCA]. | ||
==Reference== | ==Reference== | ||
Solution structure of the hDlg/SAP97 PDZ2 domain and its mechanism of interaction with HPV-18 papillomavirus E6 protein., Liu Y, Henry GD, Hegde RS, Baleja JD, Biochemistry. 2007 Sep 25;46(38):10864-74. Epub 2007 Aug 22. PMID:[http:// | Solution structure of the hDlg/SAP97 PDZ2 domain and its mechanism of interaction with HPV-18 papillomavirus E6 protein., Liu Y, Henry GD, Hegde RS, Baleja JD, Biochemistry. 2007 Sep 25;46(38):10864-74. Epub 2007 Aug 22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17713926 17713926] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: protein-peptide complex]] | [[Category: protein-peptide complex]] | ||
''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 18:03:19 2008'' | ||
Revision as of 16:03, 20 March 2008
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| Gene: | DLG1 (Homo sapiens) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Structure of the hDLG/SAP97 PDZ2 in complex with HPV-18 papillomavirus E6 peptide
Overview
The E6 protein from high-risk types of human papillomavirus (HPV) binds PDZ-domain containing proteins and targets them for degradation. We used isothermal titration calorimetry to measure the interaction of a peptide from the C-terminus of HPV-18 E6 to the second PDZ domain (PDZ2) from the human homologue of the Drosophila discs large tumor suppressor protein (hDlg). Isothermal titration calorimetry experiments with a series of peptides showed that HPV-18 E6 bound hDlg PDZ2 about 5-fold stronger than HPV-16 E6, that the contribution of Arg154 to binding was about 1 kcal/mol, and that the binding was disabled by phosphorylation at Thr156. We then used NMR to determine the solution structure of the complex of PDZ2 bound to the HPV-18 E6 peptide. The resultant structures were of high quality and had backbone root-mean-square deviations of less than 0.5 A. The structure shows a novel mode of interaction in which six residues of the HPV-18 E6 peptide are contacted by the PDZ2 domain, in contrast to the typical four residues used by class I PDZ domains. Molecular dynamics simulations supported a model in which the C- and N-terminal ends of the peptide had different mobilities within the complex. Comparison of the NMR complex structure to previously determined X-ray structures of PDZ2 by itself and bound to different peptides allows a description of conformational changes required for PDZ2 to bind to HPV-18 E6.
About this Structure
2OQS is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of the hDlg/SAP97 PDZ2 domain and its mechanism of interaction with HPV-18 papillomavirus E6 protein., Liu Y, Henry GD, Hegde RS, Baleja JD, Biochemistry. 2007 Sep 25;46(38):10864-74. Epub 2007 Aug 22. PMID:17713926
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