TY - JOUR
T1 - Structural basis for cooperativity in recruitment of MAML coactivators to Notch transcription complexes
AU - Nam, Yunsun
AU - Sliz, Piotr
AU - Song, Luyan
AU - Aster, Jon C.
AU - Blacklow, Stephen C.
N1 - Funding Information:
We thank Dr. Michael J. Eck and Dr. Stephen C. Harrison for helpful discussions, sharing facilities, and critical review of the manuscript. We are grateful to Deborah Kelly and Tom Walz for evaluating the quality of protein complexes by electron microscopy. This work was supported by NIH grants CA92433 and CA119130 (to S.C.B.) and the HHMI (P.S.). Use of the Argonne National Laboratory Structural Biology Center beamline 19ID was supported by the US Department of Energy (DOE) and of the Brookhaven National Laboratory beamline X29A by DOE and NIH.
PY - 2006/3/10
Y1 - 2006/3/10
N2 - Notch receptors transduce essential developmental signals between neighboring cells by forming a complex that leads to transcription of target genes upon activation. We report here the crystal structure of a Notch transcriptional activation complex containing the ankyrin domain of human Notch1 (ANK), the transcription factor CSL on cognate DNA, and a polypeptide from the coactivator Mastermind-like-1 (MAML-1). Together, CSL and ANK create a groove to bind the MAML-1 polypeptide as a kinked, 70 Å helix. The composite binding surface likely restricts the recruitment of MAML proteins to promoters on which Notch:CSL complexes have been preassembled, ensuring tight transcriptional control of Notch target genes.
AB - Notch receptors transduce essential developmental signals between neighboring cells by forming a complex that leads to transcription of target genes upon activation. We report here the crystal structure of a Notch transcriptional activation complex containing the ankyrin domain of human Notch1 (ANK), the transcription factor CSL on cognate DNA, and a polypeptide from the coactivator Mastermind-like-1 (MAML-1). Together, CSL and ANK create a groove to bind the MAML-1 polypeptide as a kinked, 70 Å helix. The composite binding surface likely restricts the recruitment of MAML proteins to promoters on which Notch:CSL complexes have been preassembled, ensuring tight transcriptional control of Notch target genes.
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U2 - 10.1016/j.cell.2005.12.037
DO - 10.1016/j.cell.2005.12.037
M3 - Article
C2 - 16530044
AN - SCOPUS:33644749306
SN - 0092-8674
VL - 124
SP - 973
EP - 983
JO - Cell
JF - Cell
IS - 5
ER -