1y66
From Proteopedia
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[[Image:1y66.gif|left|200px]] | [[Image:1y66.gif|left|200px]] | ||
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'''Dioxane contributes to the altered conformation and oligomerization state of a designed engrailed homeodomain variant''' | '''Dioxane contributes to the altered conformation and oligomerization state of a designed engrailed homeodomain variant''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | + | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Y66 OCA]. | |
==Reference== | ==Reference== | ||
Dioxane contributes to the altered conformation and oligomerization state of a designed engrailed homeodomain variant., Hom GK, Lassila JK, Thomas LM, Mayo SL, Protein Sci. 2005 Apr;14(4):1115-9. Epub 2005 Mar 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15741348 15741348] | Dioxane contributes to the altered conformation and oligomerization state of a designed engrailed homeodomain variant., Hom GK, Lassila JK, Thomas LM, Mayo SL, Protein Sci. 2005 Apr;14(4):1115-9. Epub 2005 Mar 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15741348 15741348] | ||
| - | [[Category: Escherichia coli]] | ||
| - | [[Category: Protein complex]] | ||
[[Category: Hom, G K.]] | [[Category: Hom, G K.]] | ||
[[Category: Lassila, J K.]] | [[Category: Lassila, J K.]] | ||
[[Category: Mayo, S L.]] | [[Category: Mayo, S L.]] | ||
[[Category: Thomas, L M.]] | [[Category: Thomas, L M.]] | ||
| - | [[Category: | + | [[Category: Dioxane]] |
| - | [[Category: | + | [[Category: Engrailed homeodomain]] |
| - | [[Category: | + | [[Category: Protein design]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:55:09 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 12:55, 3 May 2008
Dioxane contributes to the altered conformation and oligomerization state of a designed engrailed homeodomain variant
Overview
Our goal was to compute a stable, full-sequence design of the Drosophila melanogaster engrailed homeodomain. Thermal and chemical denaturation data indicated the design was significantly more stable than was the wild-type protein. The data were also nearly identical to those for a similar, later full-sequence design, which was shown by NMR to adopt the homeodomain fold: a three-helix, globular monomer. However, a 1.65 A crystal structure of the design described here turned out to be of a completely different fold: a four-helix, rodlike tetramer. The crystallization conditions included approximately 25% dioxane, and subsequent experiments by circular dichroism and sedimentation velocity analytical ultracentrifugation indicated that dioxane increases the helicity and oligomerization state of the designed protein. We attribute at least part of the discrepancy between the target fold and the crystal structure to the presence of a high concentration of dioxane.
About this Structure
Full crystallographic information is available from OCA.
Reference
Dioxane contributes to the altered conformation and oligomerization state of a designed engrailed homeodomain variant., Hom GK, Lassila JK, Thomas LM, Mayo SL, Protein Sci. 2005 Apr;14(4):1115-9. Epub 2005 Mar 1. PMID:15741348 Page seeded by OCA on Sat May 3 15:55:09 2008
