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2i13

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(New page: 200px<br /><applet load="2i13" size="450" color="white" frame="true" align="right" spinBox="true" caption="2i13, resolution 1.960&Aring;" /> '''Aart, a six finger ...)
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caption="2i13, resolution 1.960&Aring;" />
'''Aart, a six finger zinc finger designed to recognize ANN triplets'''<br />
'''Aart, a six finger zinc finger designed to recognize ANN triplets'''<br />
==Overview==
==Overview==
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Cys2-His2 zinc fingers are one of the most common types of DNA-binding, domains. Modifications to zinc-finger binding specificity have recently, enabled custom DNA-binding proteins to be designed to a wide array of, target sequences. We present here a 1.96 A structure of Aart, a designed, six-zinc finger protein, bound to a consensus DNA target site. This is the, first structure of a designed protein with six fingers, and was intended, to provide insights into the unusual affinity and specificity, characteristics of this protein. Most protein-DNA contacts were found to, be consistent with expectations, while others were unanticipated or, insufficient to explain specificity. Several were unexpectedly mediated by, glycerol, water molecules or amino acid-base stacking interactions. These, results challenge some conventional concepts of recognition, particularly, the finding that triplets containing 5'A, C, or T are typically not, specified by direct interaction with the amino acid in position 6 of the, recognition helix.
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Cys2-His2 zinc fingers are one of the most common types of DNA-binding domains. Modifications to zinc-finger binding specificity have recently enabled custom DNA-binding proteins to be designed to a wide array of target sequences. We present here a 1.96 A structure of Aart, a designed six-zinc finger protein, bound to a consensus DNA target site. This is the first structure of a designed protein with six fingers, and was intended to provide insights into the unusual affinity and specificity characteristics of this protein. Most protein-DNA contacts were found to be consistent with expectations, while others were unanticipated or insufficient to explain specificity. Several were unexpectedly mediated by glycerol, water molecules or amino acid-base stacking interactions. These results challenge some conventional concepts of recognition, particularly the finding that triplets containing 5'A, C, or T are typically not specified by direct interaction with the amino acid in position 6 of the recognition helix.
==About this Structure==
==About this Structure==
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2I13 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with ZN and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2I13 OCA].
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2I13 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=ZN:'>ZN</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=2I13 OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Bhakta, M.]]
[[Category: Bhakta, M.]]
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[[Category: Crotty, J.W.]]
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[[Category: Crotty, J W.]]
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[[Category: Horton, N.C.]]
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[[Category: Horton, N C.]]
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[[Category: III, C.F.Barbas.]]
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[[Category: III, C F.Barbas.]]
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[[Category: Segal, D.J.]]
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[[Category: Segal, D J.]]
[[Category: GOL]]
[[Category: GOL]]
[[Category: ZN]]
[[Category: ZN]]
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[[Category: zinc finger]]
[[Category: zinc finger]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 12:05:40 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:47:55 2008''

Revision as of 15:47, 21 February 2008


2i13, resolution 1.960Å

Drag the structure with the mouse to rotate

Aart, a six finger zinc finger designed to recognize ANN triplets

Overview

Cys2-His2 zinc fingers are one of the most common types of DNA-binding domains. Modifications to zinc-finger binding specificity have recently enabled custom DNA-binding proteins to be designed to a wide array of target sequences. We present here a 1.96 A structure of Aart, a designed six-zinc finger protein, bound to a consensus DNA target site. This is the first structure of a designed protein with six fingers, and was intended to provide insights into the unusual affinity and specificity characteristics of this protein. Most protein-DNA contacts were found to be consistent with expectations, while others were unanticipated or insufficient to explain specificity. Several were unexpectedly mediated by glycerol, water molecules or amino acid-base stacking interactions. These results challenge some conventional concepts of recognition, particularly the finding that triplets containing 5'A, C, or T are typically not specified by direct interaction with the amino acid in position 6 of the recognition helix.

About this Structure

2I13 is a Single protein structure of sequence from Mus musculus with and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of Aart, a designed six-finger zinc finger peptide, bound to DNA., Segal DJ, Crotty JW, Bhakta MS, Barbas CF 3rd, Horton NC, J Mol Biol. 2006 Oct 20;363(2):405-21. Epub 2006 Aug 11. PMID:16963084

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