1TOZ
NMR structure of the human NOTCH-1 ligand binding region
Summary for 1TOZ
| Entry DOI | 10.2210/pdb1toz/pdb |
| Related | 1EMO 1HJ7 1LMJ |
| Descriptor | Neurogenic locus notch homolog protein 1 (1 entity in total) |
| Functional Keywords | notch, egf, calcium binding, ligand binding, module, signaling protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Cell membrane; Single-pass type I membrane protein (By similarity). Notch 1 intracellular domain: Nucleus (By similarity): P46531 |
| Total number of polymer chains | 1 |
| Total formula weight | 12600.01 |
| Authors | Hambleton, S.,Valeyev, N.Y.,Muranyi, A.,Knott, V.,Werner, J.M.,Mcmichael, A.J.,Handford, P.A.,Downing, A.K. (deposition date: 2004-06-15, release date: 2004-10-12, Last modification date: 2024-11-20) |
| Primary citation | Hambleton, S.,Valeyev, N.V.,Muranyi, A.,Knott, V.,Werner, J.M.,McMichael, A.J.,Handford, P.A.,Downing, A.K. Structural and functional properties of the human notch-1 ligand binding region STRUCTURE, 12:2173-2183, 2004 Cited by PubMed Abstract: We present NMR structural and dynamics analysis of the putative ligand binding region of human Notch-1, comprising EGF-like domains 11-13. Functional integrity of an unglycosylated, recombinant fragment was confirmed by calcium-dependent binding of tetrameric complexes to ligand-expressing cells. EGF modules 11 and 12 adopt a well-defined, rod-like orientation rigidified by calcium. The interdomain tilt is similar to that found in previously studied calcium binding EGF pairs, but the angle of twist is significantly different. This leads to an extended double-stranded beta sheet structure, spanning the two EGF modules. Based on the conservation of residues involved in interdomain hydrophobic packing, we propose this arrangement to be prototypical of a distinct class of EGF linkages. On this premise, we have constructed a model of the 36 EGF modules of the Notch extracellular domain that enables predictions to be made about the general role of calcium binding to this region. PubMed: 15576031DOI: 10.1016/j.str.2004.09.012 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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