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[[Image:1rij.gif|left|200px]]
{{Seed}}
[[Image:1rij.png|left|200px]]


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{{STRUCTURE_1rij|  PDB=1rij  |  SCENE=  }}  
{{STRUCTURE_1rij|  PDB=1rij  |  SCENE=  }}  


'''E6-bind Trp-cage (E6apn1)'''
===E6-bind Trp-cage (E6apn1)===




==Overview==
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The E6 protein from HPV type 16 binds proteins containing a seven-residue leucine-containing motif. Previous work demonstrated that peptides containing the consensus sequence are a mixture of alpha-helix and unstructured conformations. To design monomeric E6-binding peptides that are stable in aqueous solution, we used a protein grafting approach where the critical residues of the E6-binding motif of E6-associated protein, E6AP, LQELLGE, were incorporated into exposed helices of two stably folded peptide scaffolds. One series was built using the third zinc finger of the Sp1 protein, which contains a C-terminal helix. A second series was built using a Trp-cage scaffold, which contains an N-terminal helix. The chimeric peptides had very different activities in out-competing the E6-E6AP interaction. We characterized the peptides by circular dichroism spectroscopy and determined high-resolution structures by NMR methods. The E6-binding consensus motif was found to be helical in the high-quality structures, which had backbone root-mean-square deviations of less than 0.4 A. We have successfully grafted the E6-binding motif into two parent peptides to create ligands that have biological activity while preserving the stable, native fold of their scaffolds. The data also indicate that conformational change is common in E6-binding proteins during the formation of the complex with the viral E6 protein.
The line below this paragraph, {{ABSTRACT_PUBMED_15182185}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 15182185 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15182185}}


==About this Structure==
==About this Structure==
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RIJ OCA].  
Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RIJ OCA].  


==Reference==
==Reference==
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[[Category: Human papillomavirus]]
[[Category: Human papillomavirus]]
[[Category: Trp-cage]]
[[Category: Trp-cage]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 07:32:20 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 18:31:02 2008''

Revision as of 15:31, 28 July 2008

File:1rij.png

Template:STRUCTURE 1rij

E6-bind Trp-cage (E6apn1)

Template:ABSTRACT PUBMED 15182185

About this Structure

Full experimental information is available from OCA.

Reference

Design and characterization of helical peptides that inhibit the E6 protein of papillomavirus., Liu Y, Liu Z, Androphy E, Chen J, Baleja JD, Biochemistry. 2004 Jun 15;43(23):7421-31. PMID:15182185

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