This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1rim

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1rim.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1rim.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1rim| PDB=1rim | SCENE= }}
{{STRUCTURE_1rim| PDB=1rim | SCENE= }}
-
'''E6-binding zinc finger (E6apc2)'''
+
===E6-binding zinc finger (E6apc2)===
-
==Overview==
+
<!--
-
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.
 +
-->
 +
{{ABSTRACT_PUBMED_15182185}}
==About this Structure==
==About this Structure==
-
Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RIM OCA].
+
Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RIM OCA].
==Reference==
==Reference==
Line 29: Line 33:
[[Category: Human papillomavirus]]
[[Category: Human papillomavirus]]
[[Category: Zinc finger]]
[[Category: Zinc finger]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:32:38 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:26:47 2008''

Revision as of 14:26, 27 July 2008

Image:1rim.png

Template:STRUCTURE 1rim

E6-binding zinc finger (E6apc2)

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

Page seeded by OCA on Sun Jul 27 17:26:47 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1rim"
Personal tools