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| [[Image:1nkp.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1nkp| PDB=1nkp | SCENE= }} | | {{STRUCTURE_1nkp| PDB=1nkp | SCENE= }} |
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| '''Crystal structure of Myc-Max recognizing DNA'''
| | ===Crystal structure of Myc-Max recognizing DNA=== |
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| ==Overview==
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| X-ray structures of the basic/helix-loop-helix/leucine zipper (bHLHZ) domains of Myc-Max and Mad-Max heterodimers bound to their common DNA target (Enhancer or E box hexanucleotide, 5'-CACGTG-3') have been determined at 1.9 A and 2.0 A resolution, respectively. E box recognition by these two structurally similar transcription factor pairs determines whether a cell will divide and proliferate (Myc-Max) or differentiate and become quiescent (Mad-Max). Deregulation of Myc has been implicated in the development of many human cancers, including Burkitt's lymphoma, neuroblastomas, and small cell lung cancers. Both quasisymmetric heterodimers resemble the symmetric Max homodimer, albeit with marked structural differences in the coiled-coil leucine zipper regions that explain preferential homo- and heteromeric dimerization of these three evolutionarily related DNA-binding proteins. The Myc-Max heterodimer, but not its Mad-Max counterpart, dimerizes to form a bivalent heterotetramer, which explains how Myc can upregulate expression of genes with promoters bearing widely separated E boxes.
| | The line below this paragraph, {{ABSTRACT_PUBMED_12553908}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 12553908 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_12553908}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Oncogene]] | | [[Category: Oncogene]] |
| [[Category: Transcription]] | | [[Category: Transcription]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:38:53 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:38:27 2008'' |
