2hy6: Difference between revisions

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[[Image:2hy6.jpg|left|200px]]
{{Seed}}
[[Image:2hy6.png|left|200px]]


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{{STRUCTURE_2hy6|  PDB=2hy6  |  SCENE=  }}  
{{STRUCTURE_2hy6|  PDB=2hy6  |  SCENE=  }}  


'''A seven-helix coiled coil'''
===A seven-helix coiled coil===




==Overview==
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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.
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{{ABSTRACT_PUBMED_17030805}}


==About this Structure==
==About this Structure==
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[[Category: Protein design]]
[[Category: Protein design]]
[[Category: Protein structure]]
[[Category: Protein structure]]
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