3I08
Crystal structure of the S1-cleaved Notch1 Negative Regulatory Region (NRR)
Summary for 3I08
| Entry DOI | 10.2210/pdb3i08/pdb |
| Related | 2oo4 3eto |
| Descriptor | Neurogenic locus notch homolog protein 1, CALCIUM ION, CHLORIDE ION, ... (5 entities in total) |
| Functional Keywords | sea domain, lin-12 notch repeat, lnr, heterodimerization domain, hd, activator, ank repeat, calcium, cell membrane, developmental protein, differentiation, disulfide bond, egf-like domain, glycoprotein, membrane, metal-binding, notch signaling pathway, nucleus, phosphoprotein, polymorphism, receptor, transcription, transcription regulation, transmembrane, furin, t-all, leukemia, oncogene, metalloprotease, gamma-secretase, signaling protein |
| Biological source | Homo sapiens (human) More |
| Cellular location | Cell membrane; Single-pass type I membrane protein (By similarity). Notch 1 intracellular domain: Nucleus (By similarity): P46531 P46531 |
| Total number of polymer chains | 4 |
| Total formula weight | 64233.06 |
| Authors | Gordon, W.R.,Blacklow, S.C. (deposition date: 2009-06-24, release date: 2009-09-01, Last modification date: 2024-11-06) |
| Primary citation | Gordon, W.R.,Vardar-Ulu, D.,L'Heureux, S.,Ashworth, T.,Malecki, M.J.,Sanchez-Irizarry, C.,McArthur, D.G.,Histen, G.,Mitchell, J.L.,Aster, J.C.,Blacklow, S.C. Effects of S1 cleavage on the structure, surface export, and signaling activity of human Notch1 and Notch2. Plos One, 4:e6613-e6613, 2009 Cited by PubMed Abstract: Notch receptors are normally cleaved during maturation by a furin-like protease at an extracellular site termed S1, creating a heterodimer of non-covalently associated subunits. The S1 site lies within a key negative regulatory region (NRR) of the receptor, which contains three highly conserved Lin12/Notch repeats and a heterodimerization domain (HD) that interact to prevent premature signaling in the absence of ligands. Because the role of S1 cleavage in Notch signaling remains unresolved, we investigated the effect of S1 cleavage on the structure, surface trafficking and ligand-mediated activation of human Notch1 and Notch2, as well as on ligand-independent activation of Notch1 by mutations found in human leukemia. PubMed: 19701457DOI: 10.1371/journal.pone.0006613 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.2 Å) |
Structure validation
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