1yuj

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(New page: 200px<br /><applet load="1yuj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yuj" /> '''SOLUTION NMR STRUCTURE OF THE GAGA FACTOR/DN...)
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'''SOLUTION NMR STRUCTURE OF THE GAGA FACTOR/DNA COMPLEX, 50 STRUCTURES'''<br />
'''SOLUTION NMR STRUCTURE OF THE GAGA FACTOR/DNA COMPLEX, 50 STRUCTURES'''<br />
==Overview==
==Overview==
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The structure of a complex between the DNA binding domain of the GAGA, factor (GAGA-DBD) and an oligonucleotide containing its GAGAG consensus, binding site has been determined by nuclear magnetic resonance, spectroscopy. The GAGA-DBD comprises a single classical Cys2-His2 zinc, finger core, and an N-terminal extension containing two highly basic, regions, BR1 and BR2. The zinc finger core binds in the major groove and, recognizes the first three GAG bases of the consensus in a manner similar, to that seen in other classical zinc finger-DNA complexes. Unlike the, latter, which require tandem zinc finger repeats with a minimum of two, units for high affinity binding, the GAGA-DBD makes use of only a single, finger complemented by BR1 and BR2. BR2 forms a helix that interacts in, the major groove recognizing the last G of the consensus, while BR1 wraps, around the DNA in the minor groove and recognizes the A in the fourth, position of the consensus. The implications of the structure of the, GAGA-DBD-DNA complex for chromatin remodelling are discussed.
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The structure of a complex between the DNA binding domain of the GAGA factor (GAGA-DBD) and an oligonucleotide containing its GAGAG consensus binding site has been determined by nuclear magnetic resonance spectroscopy. The GAGA-DBD comprises a single classical Cys2-His2 zinc finger core, and an N-terminal extension containing two highly basic regions, BR1 and BR2. The zinc finger core binds in the major groove and recognizes the first three GAG bases of the consensus in a manner similar to that seen in other classical zinc finger-DNA complexes. Unlike the latter, which require tandem zinc finger repeats with a minimum of two units for high affinity binding, the GAGA-DBD makes use of only a single finger complemented by BR1 and BR2. BR2 forms a helix that interacts in the major groove recognizing the last G of the consensus, while BR1 wraps around the DNA in the minor groove and recognizes the A in the fourth position of the consensus. The implications of the structure of the GAGA-DBD-DNA complex for chromatin remodelling are discussed.
==About this Structure==
==About this Structure==
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1YUJ 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1YUJ OCA].
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1YUJ 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=1YUJ OCA].
==Reference==
==Reference==
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[[Category: Drosophila melanogaster]]
[[Category: Drosophila melanogaster]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Clore, G.M.]]
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[[Category: Clore, G M.]]
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[[Category: Gronenborn, A.M.]]
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[[Category: Gronenborn, A M.]]
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[[Category: Omichinski, J.G.]]
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[[Category: Omichinski, J G.]]
[[Category: ZN]]
[[Category: ZN]]
[[Category: chromatin remodeling]]
[[Category: chromatin remodeling]]
[[Category: complex (dna-binding protein/dna)]]
[[Category: complex (dna-binding protein/dna)]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:03:37 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:09:13 2008''

Revision as of 14:09, 21 February 2008


1yuj

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SOLUTION NMR STRUCTURE OF THE GAGA FACTOR/DNA COMPLEX, 50 STRUCTURES

Overview

The structure of a complex between the DNA binding domain of the GAGA factor (GAGA-DBD) and an oligonucleotide containing its GAGAG consensus binding site has been determined by nuclear magnetic resonance spectroscopy. The GAGA-DBD comprises a single classical Cys2-His2 zinc finger core, and an N-terminal extension containing two highly basic regions, BR1 and BR2. The zinc finger core binds in the major groove and recognizes the first three GAG bases of the consensus in a manner similar to that seen in other classical zinc finger-DNA complexes. Unlike the latter, which require tandem zinc finger repeats with a minimum of two units for high affinity binding, the GAGA-DBD makes use of only a single finger complemented by BR1 and BR2. BR2 forms a helix that interacts in the major groove recognizing the last G of the consensus, while BR1 wraps around the DNA in the minor groove and recognizes the A in the fourth position of the consensus. The implications of the structure of the GAGA-DBD-DNA complex for chromatin remodelling are discussed.

About this Structure

1YUJ is a Single protein structure of sequence from Drosophila melanogaster with as ligand. Full crystallographic information is available from OCA.

Reference

The solution structure of a specific GAGA factor-DNA complex reveals a modular binding mode., Omichinski JG, Pedone PV, Felsenfeld G, Gronenborn AM, Clore GM, Nat Struct Biol. 1997 Feb;4(2):122-32. PMID:9033593

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