2drp
From Proteopedia
(New page: 200px<br /><applet load="2drp" size="450" color="white" frame="true" align="right" spinBox="true" caption="2drp, resolution 2.800Å" /> '''THE CRYSTAL STRUCTU...) |
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| - | [[Image:2drp.gif|left|200px]]<br /><applet load="2drp" size=" | + | [[Image:2drp.gif|left|200px]]<br /><applet load="2drp" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2drp, resolution 2.800Å" /> | caption="2drp, resolution 2.800Å" /> | ||
'''THE CRYSTAL STRUCTURE OF A TWO ZINC-FINGER PEPTIDE REVEALS AN EXTENSION TO THE RULES FOR ZINC-FINGER/DNA RECOGNITION'''<br /> | '''THE CRYSTAL STRUCTURE OF A TWO ZINC-FINGER PEPTIDE REVEALS AN EXTENSION TO THE RULES FOR ZINC-FINGER/DNA RECOGNITION'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The Cys2-His2 zinc-finger is the most widely occurring DNA-binding motif. | + | The Cys2-His2 zinc-finger is the most widely occurring DNA-binding motif. The first structure of a zinc-finger/DNA complex revealed a fairly simple mechanism for DNA recognition suggesting that the zinc-finger might represent a candidate template for designing proteins to recognize DNA. Residues at three key positions in an alpha-helical 'reading head' play a dominant role in base-recognition and have been targets for mutagenesis experiments aimed at deriving a recognition code. Here we report the structure of a two zinc-finger DNA-binding domain from the protein Tramtrack complexed with DNA. The amino-terminal zinc-finger and its interaction with DNA illustrate several novel features. These include the use of a serine residue, which is semi-conserved and located outside the three key positions, to make a base contact. Its role in base-recognition correlates with a large, local, protein-induced deformation of the DNA helix at a flexible A-T-A sequence and may give insight into previous mutagenesis experiments. It is apparent from this structure that zinc-finger/DNA recognition is more complex than was originally perceived. |
==About this Structure== | ==About this Structure== | ||
| - | 2DRP 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 ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 2DRP 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=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2DRP OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Chapman, L.]] | [[Category: Chapman, L.]] | ||
[[Category: Fairall, L.]] | [[Category: Fairall, L.]] | ||
| - | [[Category: Finch, J | + | [[Category: Finch, J T.]] |
[[Category: Rhodes, D.]] | [[Category: Rhodes, D.]] | ||
| - | [[Category: Schwabe, J | + | [[Category: Schwabe, J W.R.]] |
[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: double helix]] | [[Category: double helix]] | ||
[[Category: protein-dna complex]] | [[Category: protein-dna complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:01:53 2008'' |
Revision as of 15:01, 21 February 2008
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THE CRYSTAL STRUCTURE OF A TWO ZINC-FINGER PEPTIDE REVEALS AN EXTENSION TO THE RULES FOR ZINC-FINGER/DNA RECOGNITION
Overview
The Cys2-His2 zinc-finger is the most widely occurring DNA-binding motif. The first structure of a zinc-finger/DNA complex revealed a fairly simple mechanism for DNA recognition suggesting that the zinc-finger might represent a candidate template for designing proteins to recognize DNA. Residues at three key positions in an alpha-helical 'reading head' play a dominant role in base-recognition and have been targets for mutagenesis experiments aimed at deriving a recognition code. Here we report the structure of a two zinc-finger DNA-binding domain from the protein Tramtrack complexed with DNA. The amino-terminal zinc-finger and its interaction with DNA illustrate several novel features. These include the use of a serine residue, which is semi-conserved and located outside the three key positions, to make a base contact. Its role in base-recognition correlates with a large, local, protein-induced deformation of the DNA helix at a flexible A-T-A sequence and may give insight into previous mutagenesis experiments. It is apparent from this structure that zinc-finger/DNA recognition is more complex than was originally perceived.
About this Structure
2DRP is a Single protein structure of sequence from Drosophila melanogaster with as ligand. Full crystallographic information is available from OCA.
Reference
The crystal structure of a two zinc-finger peptide reveals an extension to the rules for zinc-finger/DNA recognition., Fairall L, Schwabe JW, Chapman L, Finch JT, Rhodes D, Nature. 1993 Dec 2;366(6454):483-7. PMID:8247159
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