1mdy: Difference between revisions

Revision as of 00:55, 3 May 2008

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

OverviewOverview

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.

About this StructureAbout this Structure

1MDY is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of MyoD bHLH domain-DNA complex: perspectives on DNA recognition and implications for transcriptional activation., Ma PC, Rould MA, Weintraub H, Pabo CO, Cell. 1994 May 6;77(3):451-9. PMID:8181063 Page seeded by OCA on Sat May 3 00:55:38 2008

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OCA

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 '''CRYSTAL STRUCTURE OF MYOD BHLH DOMAIN BOUND TO DNA: PERSPECTIVES ON DNA RECOGNITION AND IMPLICATIONS FOR TRANSCRIPTIONAL ACTIVATION'''
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 [[Category: Rould, M A.]]
 [[Category: Weintraub, H.]]
-[[Category: protein-dna complex]]
+[[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 Sun Mar 30 22:14:55 2008''