Notch-Jagged complex structure implicates a catch bond in tuning ligand sensitivity

Notch receptor activation initiates cell fate decisions and is distinctive in its reliance on mechanical force and protein glycosylation. The 2.5-angstrom-resolution crystal structure of the extracellular interacting region of Notch1 complexed with an engineered, high-affinity variant of Jagged1 (Ja...

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Veröffentlicht in:	Science (American Association for the Advancement of Science) 2017-03, Vol.355 (6331), p.1320-1324
Hauptverfasser:	Luca, Vincent C., Kim, Byoung Choul, Ge, Chenghao, Kakuda, Shinako, Wu, Di, Roein-Peikar, Mehdi, Haltiwanger, Robert S., Zhu, Cheng, Ha, Taekjip, Garcia, K. Christopher
Format:	Artikel
Sprache:	eng
Schlagworte:	Activation Affinity Animals Binding Bonding Cell activation Cell fate Crystal structure Crystallography, X-Ray Epidermal growth factor Fucose Fucose - chemistry Genetic Engineering Glycosylation Growth factors Intracellular Signaling Peptides and Proteins - chemistry Jagged-1 Protein - chemistry Jagged-1 Protein - genetics Jagged-1 Protein - ultrastructure Jagged1 protein Ligands Membrane Proteins - chemistry Notch sensitivity Notch1 protein Notches Polysaccharides Protein Binding Protein Domains Proteins Rats Receptor mechanisms Receptor, Notch1 - chemistry Receptor, Notch1 - genetics Receptor, Notch1 - ultrastructure Receptors Saccharomyces cerevisiae Signal Transduction Signaling
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