1an2: Difference between revisions

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[[Image:1an2.gif|left|200px]]
{{Seed}}
[[Image:1an2.png|left|200px]]


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{{STRUCTURE_1an2|  PDB=1an2  |  SCENE=  }}  
{{STRUCTURE_1an2|  PDB=1an2  |  SCENE=  }}  


'''RECOGNITION BY MAX OF ITS COGNATE DNA THROUGH A DIMERIC B/HLH/Z DOMAIN'''
===RECOGNITION BY MAX OF ITS COGNATE DNA THROUGH A DIMERIC B/HLH/Z DOMAIN===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_8479534}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 8479534 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8479534}}


==About this Structure==
==About this Structure==
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[[Category: Double helix]]
[[Category: Double helix]]
[[Category: Protein-dna complex]]
[[Category: Protein-dna complex]]
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