1an2
From Proteopedia
(New page: 200px<br /> <applet load="1an2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1an2, resolution 2.900Å" /> '''RECOGNITION BY MAX...) |
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| - | [[Image:1an2.gif|left|200px]]<br /> | + | [[Image:1an2.gif|left|200px]]<br /><applet load="1an2" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1an2" size=" | + | |
caption="1an2, resolution 2.900Å" /> | caption="1an2, resolution 2.900Å" /> | ||
'''RECOGNITION BY MAX OF ITS COGNATE DNA THROUGH A DIMERIC B/HLH/Z DOMAIN'''<br /> | '''RECOGNITION BY MAX OF ITS COGNATE DNA THROUGH A DIMERIC B/HLH/Z DOMAIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structure of the basic/helix-loop-helix/leucine | + | The three-dimensional structure of the basic/helix-loop-helix/leucine zipper domain of the transcription factor Max complexed with DNA has been determined by X-ray crystallography at 2.9 A resolution. Max binds as a dimer to its recognition sequence CACGTG by direct contacts between the alpha-helical basic region and the major groove. This symmetric homodimer, a new protein fold, is a parallel, left-handed, four-helix bundle, with each monomer containing two alpha-helical segments separated by a loop. The two alpha-helical segments are composed of the basic region plus helix 1 and helix 2 plus the leucine repeat, respectively. As in GCN4, the leucine repeat forms a parallel coiled coil. |
==About this Structure== | ==About this Structure== | ||
| - | 1AN2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | + | 1AN2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AN2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: ]] | [[Category: ]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Amare, A | + | [[Category: Amare, A R.Ferre-D.]] |
| - | [[Category: Burley, S | + | [[Category: Burley, S K.]] |
| - | [[Category: Prendergast, G | + | [[Category: Prendergast, G C.]] |
| - | [[Category: Ziff, E | + | [[Category: Ziff, E B.]] |
[[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 11:46:22 2008'' |
Revision as of 09:46, 21 February 2008
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RECOGNITION BY MAX OF ITS COGNATE DNA THROUGH A DIMERIC B/HLH/Z DOMAIN
Overview
The three-dimensional structure of the basic/helix-loop-helix/leucine zipper domain of the transcription factor Max complexed with DNA has been determined by X-ray crystallography at 2.9 A resolution. Max binds as a dimer to its recognition sequence CACGTG by direct contacts between the alpha-helical basic region and the major groove. This symmetric homodimer, a new protein fold, is a parallel, left-handed, four-helix bundle, with each monomer containing two alpha-helical segments separated by a loop. The two alpha-helical segments are composed of the basic region plus helix 1 and helix 2 plus the leucine repeat, respectively. As in GCN4, the leucine repeat forms a parallel coiled coil.
About this Structure
1AN2 is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Recognition by Max of its cognate DNA through a dimeric b/HLH/Z domain., Ferre-D'Amare AR, Prendergast GC, Ziff EB, Burley SK, Nature. 1993 May 6;363(6424):38-45. PMID:8479534 [[Category: ]]
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