2hot
From Proteopedia
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- | [[Image:2hot.gif|left|200px]] | + | [[Image:2hot.gif|left|200px]] |
- | + | ||
- | '''Phage selected homeodomain bound to modified DNA''' | + | {{Structure |
+ | |PDB= 2hot |SIZE=350|CAPTION= <scene name='initialview01'>2hot</scene>, resolution 2.19Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=P2O:3-PROP-2-YN-1-YL-1,3-OXAZOLIDIN-2-ONE'>P2O</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= En ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 Drosophila melanogaster]) | ||
+ | }} | ||
+ | |||
+ | '''Phage selected homeodomain bound to modified DNA''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 2HOT is a [ | + | 2HOT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HOT OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17240973 17240973] |
[[Category: Drosophila melanogaster]] | [[Category: Drosophila melanogaster]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: phage display]] | [[Category: phage display]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:19:36 2008'' |
Revision as of 15:19, 20 March 2008
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, resolution 2.19Å | |||||||
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Ligands: | and | ||||||
Gene: | En (Drosophila melanogaster) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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. 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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