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| - | [[Image:2hy6.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2hy6| PDB=2hy6 | SCENE= }} | | {{STRUCTURE_2hy6| PDB=2hy6 | SCENE= }} |
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| - | '''A seven-helix coiled coil'''
| + | ===A seven-helix coiled coil=== |
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| - | ==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}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[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
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
