1w5h
From Proteopedia
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[[Image:1w5h.gif|left|200px]] | [[Image:1w5h.gif|left|200px]] | ||
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| - | + | {{STRUCTURE_1w5h| PDB=1w5h | SCENE= }} | |
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'''AN ANTI-PARALLEL FOUR HELIX BUNDLE.''' | '''AN ANTI-PARALLEL FOUR HELIX BUNDLE.''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1W5H is a [[Single protein]] structure | + | 1W5H is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W5H OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Stout, C D.]] | [[Category: Stout, C D.]] | ||
[[Category: Yadav, M K.]] | [[Category: Yadav, M K.]] | ||
| - | [[Category: | + | [[Category: Antiparallel four helix bundle]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 13:11:15 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 10:11, 3 May 2008
AN ANTI-PARALLEL FOUR HELIX BUNDLE.
Overview
A detailed understanding of the mechanisms by which particular amino acid sequences can give rise to more than one folded structure, such as for proteins that undergo large conformational changes or misfolding, is a long-standing objective of protein chemistry. Here, we describe the crystal structures of a single coiled-coil peptide in distinct parallel and antiparallel tetrameric configurations and further describe the parallel or antiparallel crystal structures of several related peptide sequences; the antiparallel tetrameric assemblies represent the first crystal structures of GCN4-derived peptides exhibiting such a configuration. Intriguingly, substitution of a single solvent-exposed residue enabled the parallel coiled-coil tetramer GCN4-pLI to populate the antiparallel configuration, suggesting that the two configurations are close enough in energy for subtle sequence changes to have important structural consequences. We present a structural analysis of the small changes to the helix register and side-chain conformations that accommodate the two configurations and have supplemented these results using solution studies and a molecular dynamics energetic analysis using a replica exchange methodology. Considering the previous examples of structural nonspecificity in coiled-coil peptides, the findings reported here not only emphasize the predisposition of the coiled-coil motif to adopt multiple configurations but also call attention to the associated risk that observed crytstal structures may not represent the only (or even the major) species present in solution.
About this Structure
1W5H is a Single protein structure. Full crystallographic information is available from OCA.
Reference
Coiled coils at the edge of configurational heterogeneity. Structural analyses of parallel and antiparallel homotetrameric coiled coils reveal configurational sensitivity to a single solvent-exposed amino acid substitution., Yadav MK, Leman LJ, Price DJ, Brooks CL 3rd, Stout CD, Ghadiri MR, Biochemistry. 2006 Apr 11;45(14):4463-73. PMID:16584182 Page seeded by OCA on Sat May 3 13:11:15 2008
