2fo1
From Proteopedia
Crystal Structure of the CSL-Notch-Mastermind ternary complex bound to DNA
Structural highlights
Function[LAG3_CAEEL] Glp-1 and lin-12 promote signalling by recruiting lag-3 to target promoters, where it functions as a transcriptional activator. [LIN12_CAEEL] Involved in several cell fate decisions that require cell-cell interactions. It is possible that lin-12 encodes a membrane-bound receptor for a signal that enables expression of the ventral uterine precursor cell fate. Activity in cell fate decisions and tumorigenesis is negatively regulated by sel-10.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedNotch signaling mediates communication between cells and is essential for proper embryonic patterning and development. CSL is a DNA binding transcription factor that regulates transcription of Notch target genes by interacting with coregulators. Transcriptional activation requires the displacement of corepressors from CSL by the intracellular portion of the receptor Notch (NotchIC) and the recruitment of the coactivator protein Mastermind to the complex. Here we report the 3.1 A structure of the ternary complex formed by CSL, NotchIC, and Mastermind bound to DNA. As expected, the RAM domain of Notch interacts with the beta trefoil domain of CSL; however, the C-terminal domain of CSL has an unanticipated central role in the interface formed with the Notch ankyrin repeats and Mastermind. Ternary complex formation induces a substantial conformational change within CSL, suggesting a molecular mechanism for the conversion of CSL from a repressor to an activator. Crystal structure of the CSL-Notch-Mastermind ternary complex bound to DNA.,Wilson JJ, Kovall RA Cell. 2006 Mar 10;124(5):985-96. PMID:16530045[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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