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1y66

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{{STRUCTURE_1y66| PDB=1y66 | SCENE= }}
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'''Dioxane contributes to the altered conformation and oligomerization state of a designed engrailed homeodomain variant'''
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===Dioxane contributes to the altered conformation and oligomerization state of a designed engrailed homeodomain variant===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 15741348 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15741348}}
==About this Structure==
==About this Structure==
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[[Category: Engrailed homeodomain]]
[[Category: Engrailed homeodomain]]
[[Category: Protein design]]
[[Category: Protein design]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:55:09 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:53:38 2008''

Revision as of 23:53, 28 July 2008

Image:1y66.png

Template:STRUCTURE 1y66

Dioxane contributes to the altered conformation and oligomerization state of a designed engrailed homeodomain variant

Template:ABSTRACT PUBMED 15741348

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 Tue Jul 29 02:53:38 2008

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