1mdy: Difference between revisions

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[[Image:1mdy.~~gif~~|left|200px]]

[[Image:1mdy.png|left|200px]]

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~~'''~~CRYSTAL STRUCTURE OF MYOD BHLH DOMAIN BOUND TO DNA: PERSPECTIVES ON DNA RECOGNITION AND IMPLICATIONS FOR TRANSCRIPTIONAL ACTIVATION~~'''~~

===CRYSTAL STRUCTURE OF MYOD BHLH DOMAIN BOUND TO DNA: PERSPECTIVES ON DNA RECOGNITION AND IMPLICATIONS FOR TRANSCRIPTIONAL ACTIVATION===

~~==Overview==~~

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The ~~crystal structure of a MyoD basic-helix-loop-helix~~ (~~bHLH) domain-DNA complex has been solved and refined~~ at 2.~~8 A resolution~~. ~~This structure proves that bHLH and bHLH-leucine zipper (bHLH-ZIP~~) proteins are remarkably similar; it helps us understand subtle differences in binding preferences for these proteins; and it has surprising implications for our understanding of transcription. Specifically, ~~Ala-114 and Thr-115, which are required for positive control in the myogenic proteins, are buried at~~ the ~~protein-DNA interface~~. ~~These residues are not available for direct protein~~-~~protein contacts, but they may determine the conformation of Arg~~-~~111. Comparisons with Max suggest that the conformation of this arginine, which is different in the two structures, may play an important role in myogenic transcription.~~

The line below this paragraph, {{ABSTRACT_PUBMED_8181063}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 8181063 is the PubMed ID number.

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==About this Structure==

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[[Category: Weintraub, H.]]

[[Category: Protein-dna complex]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May~~ ~~3 00~~:55:38 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 23:45:48 2008''

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-[[Image:1mdy.gif|left|200px]]
+{{Seed}}
+[[Image:1mdy.png|left|200px]]
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 {{STRUCTURE_1mdy|  PDB=1mdy  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF MYOD BHLH DOMAIN BOUND TO DNA: PERSPECTIVES ON DNA RECOGNITION AND IMPLICATIONS FOR TRANSCRIPTIONAL ACTIVATION'''
+===CRYSTAL STRUCTURE OF MYOD BHLH DOMAIN BOUND TO DNA: PERSPECTIVES ON DNA RECOGNITION AND IMPLICATIONS FOR TRANSCRIPTIONAL ACTIVATION===
-==Overview==
+<!--
-The crystal structure of a MyoD basic-helix-loop-helix (bHLH) domain-DNA complex has been solved and refined at 2.8 A resolution. This structure proves that bHLH and bHLH-leucine zipper (bHLH-ZIP) proteins are remarkably similar; it helps us understand subtle differences in binding preferences for these proteins; and it has surprising implications for our understanding of transcription. Specifically, Ala-114 and Thr-115, which are required for positive control in the myogenic proteins, are buried at the protein-DNA interface. These residues are not available for direct protein-protein contacts, but they may determine the conformation of Arg-111. Comparisons with Max suggest that the conformation of this arginine, which is different in the two structures, may play an important role in myogenic transcription.
+The line below this paragraph, {{ABSTRACT_PUBMED_8181063}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8181063 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8181063}}
 ==About this Structure==
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 [[Category: Weintraub, H.]]
 [[Category: Protein-dna complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 00:55:38 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 23:45:48 2008''