1an2
From Proteopedia
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| - | [[Image:1an2.gif|left|200px]] | + | [[Image:1an2.gif|left|200px]] |
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| - | '''RECOGNITION BY MAX OF ITS COGNATE DNA THROUGH A DIMERIC B/HLH/Z DOMAIN''' | + | {{Structure |
| + | |PDB= 1an2 |SIZE=350|CAPTION= <scene name='initialview01'>1an2</scene>, resolution 2.900Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''RECOGNITION BY MAX OF ITS COGNATE DNA THROUGH A DIMERIC B/HLH/Z DOMAIN''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1AN2 is a [ | + | 1AN2 is a [[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== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8479534 8479534] |
[[Category: ]] | [[Category: ]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: protein-dna complex]] | [[Category: protein-dna complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 09:59:48 2008'' |
Revision as of 07:59, 20 March 2008
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| , resolution 2.900Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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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