1mdy
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /><applet load="1mdy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mdy, resolution 2.800Å" /> '''CRYSTAL STRUCTURE O...)
Next diff →
Revision as of 19:14, 20 November 2007
|
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.
About this Structure
1MDY is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.
Reference
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 Tue Nov 20 21:21:20 2007
