期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 14, 期 4, 页码 295-300出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb1227
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资金
- NCI NIH HHS [R01 CA092433-04, P01 CA119070-01A19001, R01 CA092433-03, R01 CA092433-05, R01 CA092433, P01 CA119070-01A10003, R01 CA092433-05S1, P01 CA119070] Funding Source: Medline
Notch receptors transmit signals between adjacent cells. Signaling is initiated when ligand binding induces metalloprotease cleavage of Notch within an extracellular negative regulatory region (NRR). We present here the X-ray structure of the human NOTCH2 NRR, which adopts an autoinhibited conformation. Extensive interdomain interactions within the NRR bury the metalloprotease site, showing that a substantial conformational movement is necessary to expose this site during activation by ligand. Leukemia-associated mutations in NOTCH1 probably release autoinhibition by destabilizing the conserved hydrophobic core of the NRR.
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