2hot: Difference between revisions

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[[Image:2hot.gif|left|200px]]
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[[Image:2hot.png|left|200px]]


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{{STRUCTURE_2hot|  PDB=2hot  |  SCENE=  }}  
{{STRUCTURE_2hot|  PDB=2hot  |  SCENE=  }}  


'''Phage selected homeodomain bound to modified DNA'''
===Phage selected homeodomain bound to modified DNA===




==Overview==
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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.
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{{ABSTRACT_PUBMED_17240973}}


==About this Structure==
==About this Structure==
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[[Category: Homeodomain]]
[[Category: Homeodomain]]
[[Category: Phage display]]
[[Category: Phage display]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:15:31 2008''

Revision as of 03:15, 28 July 2008

File:2hot.png

Template:STRUCTURE 2hot

Phage selected homeodomain bound to modified DNA

Template:ABSTRACT PUBMED 17240973

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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