PDBsum entry 1yyh

Go to PDB code: 
protein Protein-protein interface(s) links
Cell cycle,transcription PDB id
Jmol PyMol
Protein chain
193 a.a. *
Waters ×537
* Residue conservation analysis
PDB id:
Name: Cell cycle,transcription
Title: Crystal structure of the human notch 1 ankyrin domain
Structure: Notch 1, ankyrin domain. Chain: a, b. Fragment: ankyrin domain. Synonym: neurogenic locus notch homolog protein 1. Hn1. Translocation-associated notch protein tan-1. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: notch1, tan1. Expressed in: escherichia coli. Expression_system_taxid: 562.
1.90Å     R-factor:   0.163     R-free:   0.193
Authors: M.T.Ehebauer,D.Y.Chirgadze,P.Hayward,A.Martinez-Arias, T.L.Blundell
Key ref: M.T.Ehebauer et al. (2005). High-resolution crystal structure of the human Notch 1 ankyrin domain. Biochem J, 392, 13-20. PubMed id: 16011479
25-Feb-05     Release date:   16-Aug-05    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P46531  (NOTC1_HUMAN) -  Neurogenic locus notch homolog protein 1
2555 a.a.
193 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)


Biochem J 392:13-20 (2005)
PubMed id: 16011479  
High-resolution crystal structure of the human Notch 1 ankyrin domain.
M.T.Ehebauer, D.Y.Chirgadze, P.Hayward, A.Martinez Arias, T.L.Blundell.
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.

Literature references that cite this PDB file's key reference

  PubMed id Reference
19668359 P.G.Sanders, S.Muñoz-Descalzo, T.Balayo, F.Wirtz-Peitz, P.Hayward, and A.M.Arias (2009).
Ligand-independent traffic of Notch buffers activated Armadillo in Drosophila.
  PLoS Biol, 7, e1000169.  
18480049 D.Fox, I.Le Trong, P.Rajagopal, P.S.Brzovic, R.E.Stenkamp, and R.E.Klevit (2008).
Crystal structure of the BARD1 ankyrin repeat domain and its functional consequences.
  J Biol Chem, 283, 21179-21186.
PDB code: 3c5r
18799787 W.R.Gordon, K.L.Arnett, and S.C.Blacklow (2008).
The molecular logic of Notch signaling--a structural and biochemical perspective.
  J Cell Sci, 121, 3109-3119.  
17535912 D.F.Kelly, R.J.Lake, T.Walz, and S.Artavanis-Tsakonas (2007).
Conformational variability of the intracellular domain of Drosophila Notch and its interaction with Suppressor of Hairless.
  Proc Natl Acad Sci U S A, 104, 9591-9596.  
17720975 M.A.Borzok, D.H.Catino, J.D.Nicholson, A.Kontrogianni-Konstantopoulos, and R.J.Bloch (2007).
Mapping the binding site on small ankyrin 1 for obscurin.
  J Biol Chem, 282, 32384-32396.  
17573339 M.L.Coleman, M.A.McDonough, K.S.Hewitson, C.Coles, J.Mecinovic, M.Edelmann, K.M.Cook, M.E.Cockman, D.E.Lancaster, B.M.Kessler, N.J.Oldham, P.J.Ratcliffe, and C.J.Schofield (2007).
Asparaginyl hydroxylation of the Notch ankyrin repeat domain by factor inhibiting hypoxia-inducible factor.
  J Biol Chem, 282, 24027-24038.
PDB codes: 2qc9 3p3n 3p3p
17284587 Y.Nam, P.Sliz, W.S.Pear, J.C.Aster, and S.C.Blacklow (2007).
Cooperative assembly of higher-order Notch complexes functions as a switch to induce transcription.
  Proc Natl Acad Sci U S A, 104, 2103-2108.  
16618368 K.Peng, P.Radivojac, S.Vucetic, A.K.Dunker, and Z.Obradovic (2006).
Length-dependent prediction of protein intrinsic disorder.
  BMC Bioinformatics, 7, 208.  
16397895 M.Kaspar, and T.Klein (2006).
Functional analysis of murine CBF1 during Drosophila development.
  Dev Dyn, 235, 918-927.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.