1nlw
From Proteopedia
(New page: 200px<br /> <applet load="1nlw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nlw, resolution 2.0Å" /> '''Crystal structure of...) |
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| - | [[Image:1nlw.gif|left|200px]]<br /> | + | [[Image:1nlw.gif|left|200px]]<br /><applet load="1nlw" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1nlw, resolution 2.0Å" /> | caption="1nlw, resolution 2.0Å" /> | ||
'''Crystal structure of Mad-Max recognizing DNA'''<br /> | '''Crystal structure of Mad-Max recognizing DNA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | X-ray structures of the basic/helix-loop-helix/leucine zipper (bHLHZ) | + | 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. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1NLW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1NLW is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NLW OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Burley, S | + | [[Category: Burley, S K.]] |
| - | [[Category: Nair, S | + | [[Category: Nair, S K.]] |
[[Category: bhlhz]] | [[Category: bhlhz]] | ||
[[Category: dna]] | [[Category: dna]] | ||
[[Category: transcription factor]] | [[Category: transcription factor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:07:28 2008'' |
Revision as of 12:07, 21 February 2008
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Crystal structure of Mad-Max recognizing DNA
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Lymphoma, somatic OMIM:[602686], Prostate cancer, somatic OMIM:[602686]
About this Structure
1NLW is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
X-ray structures of Myc-Max and Mad-Max recognizing DNA. Molecular bases of regulation by proto-oncogenic transcription factors., Nair SK, Burley SK, Cell. 2003 Jan 24;112(2):193-205. PMID:12553908
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