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.


2hy6

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2hy6.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2hy6.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2hy6| PDB=2hy6 | SCENE= }}
{{STRUCTURE_2hy6| PDB=2hy6 | SCENE= }}
-
'''A seven-helix coiled coil'''
+
===A seven-helix coiled coil===
-
==Overview==
+
<!--
-
Coiled-coil proteins contain a characteristic seven-residue sequence repeat whose positions are designated a to g. The interacting surface between alpha-helices in a classical coiled coil is formed by interspersing nonpolar side chains at the a and d positions with hydrophilic residues at the flanking e and g positions. To explore how the chemical nature of these core amino acids dictates the overall coiled-coil architecture, we replaced all eight e and g residues in the GCN4 leucine zipper with nonpolar alanine side chains. Surprisingly, the alanine-containing mutant forms a stable alpha-helical heptamer in aqueous solution. The 1.25-A resolution crystal structure of the heptamer reveals a parallel seven-stranded coiled coil enclosing a large tubular channel with an unusual heptad register shift between adjacent staggered helices. The overall geometry comprises two interleaved hydrophobic helical screws of interacting cross-sectional a and d layers that have not been seen before. Moreover, asparagines at the a positions play an essential role in heptamer formation by participating in a set of buried interhelix hydrogen bonds. These results demonstrate that heptad repeats containing four hydrophobic positions can direct assembly of complex, higher-order coiled-coil structures with rich diversity for close packing of alpha-helices.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17030805}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17030805 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17030805}}
==About this Structure==
==About this Structure==
Line 32: Line 36:
[[Category: Protein design]]
[[Category: Protein design]]
[[Category: Protein structure]]
[[Category: Protein structure]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:51:29 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:26:30 2008''

Revision as of 03:26, 29 July 2008

Image:2hy6.png

Template:STRUCTURE 2hy6

A seven-helix coiled coil

Template:ABSTRACT PUBMED 17030805

About this Structure

2HY6 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

A seven-helix coiled coil., Liu J, Zheng Q, Deng Y, Cheng CS, Kallenbach NR, Lu M, Proc Natl Acad Sci U S A. 2006 Oct 17;103(42):15457-62. Epub 2006 Oct 9. PMID:17030805

Page seeded by OCA on Tue Jul 29 06:26:30 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2hy6"
Personal tools