1YYH

Crystal structure of the human Notch 1 ankyrin domain

Summary for 1YYH

• Entry DOI: 10.2210/pdb1yyh/pdb
• Descriptor: Notch 1, ankyrin domain (2 entities in total)
• Functional Keywords: ankyrin repeats; notch 1, cell cycle, transcription
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 55557.69

Authors

Ehebauer, M.T.,Chirgadze, D.Y.,Hayward, P.,Martinez-Arias, A.,Blundell, T.L. (deposition date: 2005-02-25, release date: 2005-08-16, Last modification date: 2023-08-23)

Primary citation

Ehebauer, M.T.,Chirgadze, D.Y.,Hayward, P.,Martinez-Arias, A.,Blundell, T.L.
High-resolution crystal structure of the human Notch 1 ankyrin domain
Biochem.J., 392:13-20, 2005

PubMed Abstract: The Notch receptor is part of a highly conserved signalling system of central importance to animal development. Its ANK (ankyrin) domain is required for Notch-mediated signal transduction. The crystal structure of the human Notch 1 ANK domain was solved by molecular replacement at 1.9 A (1 A=0.1 nm) resolution, and it shows that the features identified in the Drosophila homologue are conserved. The domain has six of the seven ANK repeats predicted from sequence. The putative first repeat, which has only part of the consensus and a long insertion, is disordered in both molecules in the asymmetric unit, possibly due to the absence of the RAM (RBPJkappa-associated molecule) region N-terminal to it. The exposed hydrophobic core is involved in intermolecular interactions in the crystal. Evolutionary trace analysis identified several residues that map to the hairpins of the structure and may be of functional importance. Based on the Notch 1 ANK structure and analysis of homologous Notch ANK sequences, we predict two possible binding sites on the domain: one on the concave surface of repeat 2 and the other below the hairpins of repeats 6-7.

PubMed: 16011479
DOI: 10.1042/BJ20050515

Experimental method

X-RAY DIFFRACTION (1.901 Å)