Structural basis for autoinhibition of Notch View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2007-04-01

AUTHORS

Wendy R Gordon, Didem Vardar-Ulu, Gavin Histen, Cheryll Sanchez-Irizarry, Jon C Aster, Stephen C Blacklow

ABSTRACT

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. More... »

PAGES

295-300

Journal

TITLE

Nature Structural & Molecular Biology

ISSUE

4

VOLUME

14

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/nsmb1227

    DOI

    http://dx.doi.org/10.1038/nsmb1227

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1014955709

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/17401372


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