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==Overview==

C-terminal-binding protein/brefeldin A-ADP ribosylated substrate, (CtBP/BARS) plays key roles in development and oncogenesis as a, transcription co-repressor, and in intracellular traffic as a promoter of, Golgi membrane fission. Co-repressor activity is regulated by NAD(H), binding to CtBP/BARS, while membrane fission is associated with its, acyl-CoA-dependent acyltransferase activity. Here, we report the crystal, structures of rat CtBP/BARS in a binary complex with NAD(H), and in a, ternary complex with a PIDLSKK peptide mimicking the consensus motif, (PXDLS) recognized in CtBP/BARS cellular partners. The structural data, show CtBP/BARS in a NAD(H)-bound dimeric form; the peptide binding maps, the recognition site for DNA-binding proteins and histone deacetylases to, an N-terminal region of the protein. The crystal structure together with, the site-directed mutagenesis data and binding experiments suggest a, rationale for the molecular mechanisms underlying the two fundamental, co-existing, but diverse, activities supported by CtBP/BARS in the nucleus, and in Golgi membranes.

C-terminal-binding protein/brefeldin A-ADP ribosylated substrate (CtBP/BARS) plays key roles in development and oncogenesis as a transcription co-repressor, and in intracellular traffic as a promoter of Golgi membrane fission. Co-repressor activity is regulated by NAD(H) binding to CtBP/BARS, while membrane fission is associated with its acyl-CoA-dependent acyltransferase activity. Here, we report the crystal structures of rat CtBP/BARS in a binary complex with NAD(H), and in a ternary complex with a PIDLSKK peptide mimicking the consensus motif (PXDLS) recognized in CtBP/BARS cellular partners. The structural data show CtBP/BARS in a NAD(H)-bound dimeric form; the peptide binding maps the recognition site for DNA-binding proteins and histone deacetylases to an N-terminal region of the protein. The crystal structure together with the site-directed mutagenesis data and binding experiments suggest a rationale for the molecular mechanisms underlying the two fundamental co-existing, but diverse, activities supported by CtBP/BARS in the nucleus and in Golgi membranes.

==About this Structure==

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[[Category: transcription co-repression]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:02:23 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-C-terminal-binding protein/brefeldin A-ADP ribosylated substrate, (CtBP/BARS) plays key roles in development and oncogenesis as a, transcription co-repressor, and in intracellular traffic as a promoter of, Golgi membrane fission. Co-repressor activity is regulated by NAD(H), binding to CtBP/BARS, while membrane fission is associated with its, acyl-CoA-dependent acyltransferase activity. Here, we report the crystal, structures of rat CtBP/BARS in a binary complex with NAD(H), and in a, ternary complex with a PIDLSKK peptide mimicking the consensus motif, (PXDLS) recognized in CtBP/BARS cellular partners. The structural data, show CtBP/BARS in a NAD(H)-bound dimeric form; the peptide binding maps, the recognition site for DNA-binding proteins and histone deacetylases to, an N-terminal region of the protein. The crystal structure together with, the site-directed mutagenesis data and binding experiments suggest a, rationale for the molecular mechanisms underlying the two fundamental, co-existing, but diverse, activities supported by CtBP/BARS in the nucleus, and in Golgi membranes.
+C-terminal-binding protein/brefeldin A-ADP ribosylated substrate (CtBP/BARS) plays key roles in development and oncogenesis as a transcription co-repressor, and in intracellular traffic as a promoter of Golgi membrane fission. Co-repressor activity is regulated by NAD(H) binding to CtBP/BARS, while membrane fission is associated with its acyl-CoA-dependent acyltransferase activity. Here, we report the crystal structures of rat CtBP/BARS in a binary complex with NAD(H), and in a ternary complex with a PIDLSKK peptide mimicking the consensus motif (PXDLS) recognized in CtBP/BARS cellular partners. The structural data show CtBP/BARS in a NAD(H)-bound dimeric form; the peptide binding maps the recognition site for DNA-binding proteins and histone deacetylases to an N-terminal region of the protein. The crystal structure together with the site-directed mutagenesis data and binding experiments suggest a rationale for the molecular mechanisms underlying the two fundamental co-existing, but diverse, activities supported by CtBP/BARS in the nucleus and in Golgi membranes.
 ==About this Structure==
@@ Line 30: / Line 30: @@
 [[Category: transcription co-repression]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb  3 09:50:05 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:02:23 2008''