2hot
From Proteopedia
(New page: 200px<br /><applet load="2hot" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hot, resolution 2.19Å" /> '''Phage selected homeo...) |
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| - | [[Image:2hot.gif|left|200px]]<br /><applet load="2hot" size=" | + | [[Image:2hot.gif|left|200px]]<br /><applet load="2hot" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2hot, resolution 2.19Å" /> | caption="2hot, resolution 2.19Å" /> | ||
'''Phage selected homeodomain bound to modified DNA'''<br /> | '''Phage selected homeodomain bound to modified DNA'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2HOT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with P2O and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 2HOT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with <scene name='pdbligand=P2O:'>P2O</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HOT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: phage display]] | [[Category: phage display]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 15:18:25 2008'' |
Revision as of 13:18, 23 January 2008
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Phage selected homeodomain bound to modified DNA
Overview
The homeodomain (HD)-DNA interface has been conserved over 500 million, years of evolution. Despite this conservation, we have successfully, re-engineered the engrailed HD to specifically recognize an unnatural, nucleotide using a phage display selection. Here we report the synthesis, of novel nucleosides and the selection of mutant HDs that bind these, nucleotides using phage display. The high-resolution crystal structure of, one mutant in complex with modified and unmodified DNA demonstrates that, even with the substantial perturbation to the interface, this selected, mutant retains a canonical HD structure. Dissection of the contributions, due to each of the selected mutations reveals that the majority of the, modification-specific binding is accomplished by a single mutation (I47G), but that the remaining mutations retune the stability of the HD. These, results afford a detailed look at a re-engineered protein-DNA interaction, and provide insight into the opportunities for re-engineering highly, conserved interfaces.
About this Structure
2HOT is a Single protein structure of sequence from Drosophila melanogaster with and as ligands. Full crystallographic information is available from OCA.
Reference
Structure and properties of a re-engineered homeodomain protein-DNA interface., Simon MD, Feldman ME, Rauh D, Maris AE, Wemmer DE, Shokat KM, ACS Chem Biol. 2006 Dec 15;1(12):755-60. PMID:17240973
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