spacer
spacer

PDBsum entry 1ymp
Go to PDB code: 
protein Protein-protein interface(s) links
Transcription PDB id
1ymp

 

 

 

 

Loading ...

 
JSmol PyMol  
Contents
Protein chains
131 a.a. *
Waters ×149
* Residue conservation analysis
PDB id:
1ymp
Name: Transcription
Title: The crystal structure of a partial mouse notch-1 ankyrin domain: repeats 4 through 7 preserve an ankyrin fold
Structure: Notch 1 protein. Chain: a, b. Fragment: ankryin repeats 3.5-7 (residues 1971-2105). Engineered: yes
Source: Mus musculus. House mouse. Organism_taxid: 10090. Gene: notch1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Biol. unit: Dimer (from PQS)
Resolution:
2.20Å     R-factor:   0.206     R-free:   0.309
Authors: O.Y.Lubman,R.Kopan,G.Waksman,S.Korolev
Key ref:
O.Y.Lubman et al. (2005). The crystal structure of a partial mouse Notch-1 ankyrin domain: repeats 4 through 7 preserve an ankyrin fold. Protein Sci, 14, 1274-1281. PubMed id: 15802643 DOI: 10.1110/ps.041184105
Date:
21-Jan-05     Release date:   10-May-05    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q01705  (NOTC1_MOUSE) -  Neurogenic locus notch homolog protein 1 from Mus musculus
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		2531 a.a.
131 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 

 
DOI no: 10.1110/ps.041184105 Protein Sci 14:1274-1281 (2005)
PubMed id: 15802643  
 
 
The crystal structure of a partial mouse Notch-1 ankyrin domain: repeats 4 through 7 preserve an ankyrin fold.
O.Y.Lubman, R.Kopan, G.Waksman, S.Korolev.
 
  ABSTRACT  
 
Folding and stability of proteins containing ankyrin repeats (ARs) is of great interest because they mediate numerous protein-protein interactions involved in a wide range of regulatory cellular processes. Notch, an ankyrin domain containing protein, signals by converting a transcriptional repression complex into an activation complex. The Notch ANK domain is essential for Notch function and contains seven ARs. Here, we present the 2.2 A crystal structure of ARs 4-7 from mouse Notch 1 (m1ANK). These C-terminal repeats were resistant to degradation during crystallization, and their secondary and tertiary structures are maintained in the absence of repeats 1-3. The crystallized fragment adopts a typical ankyrin fold including the poorly conserved seventh AR, as seen in the Drosophila Notch ANK domain (dANK). The structural preservation and stability of the C-terminal repeats shed a new light onto the mechanism of hetero-oligomeric assembly during Notch-mediated transcriptional activation.
 
  Selected figure(s)  
 
Figure 1.
Figure 1. (A) Simplified schematic diagram of the Notch-mediated transcriptional "switch." NICD is composed of a membrane proximal RAM domain (yellow), seven ARs (red), and C-terminal PEST, OPA domains (navy). Binding of NICD to CSL displaces transcriptional repressors (SMRT, HDAC, CIR) and leads to recruitment of transcriptional activators MAM and HAT. (B) A 2.2 Å crystal structure of mouse Notch1 ARs 3 -7. There are two molecules in the asymmetric unit of the crystal. Repeats 3 -7 of molecule A are colored red, yellow, green, brown, and cyan, respectively. Repeats of molecule B are colored gray. (C) Structural overlay of partial ANK domain of mouse Notch-1 with ARs is color coded as in B and the dANK domain of the Drosophila Notch receptor is shown in a gray transparent worm representation.
 
  The above figure is reprinted by permission from the Protein Society: Protein Sci (2005, 14, 1274-1281) copyright 2005.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19962898 S.Al-Khodor, C.T.Price, A.Kalia, and Y.Abu Kwaik (2010).
Functional diversity of ankyrin repeats in microbial proteins.
  Trends Microbiol, 18, 132-139.  
19401150 S.E.Wilkins, J.Hyvärinen, J.Chicher, J.J.Gorman, D.J.Peet, R.L.Bilton, and P.Koivunen (2009).
Differences in hydroxylation and binding of Notch and HIF-1alpha demonstrate substrate selectivity for factor inhibiting HIF-1 (FIH-1).
  Int J Biochem Cell Biol, 41, 1563-1571.  
19289204 T.Aksel, and D.Barrick (2009).
Analysis of repeat-protein folding using nearest-neighbor statistical mechanical models.
  Methods Enzymol, 455, 95.  
18758478 R.A.Kovall (2008).
More complicated than it looks: assembly of Notch pathway transcription complexes.
  Oncogene, 27, 5099-5109.  
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.  
17229764 H.T.Cheng, M.Kim, M.T.Valerius, K.Surendran, K.Schuster-Gossler, A.Gossler, A.P.McMahon, and R.Kopan (2007).
Notch2, but not Notch1, is required for proximal fate acquisition in the mammalian nephron.
  Development, 134, 801-811.  
17070841 O.Y.Lubman, M.X.Ilagan, R.Kopan, and D.Barrick (2007).
Quantitative dissection of the Notch:CSL interaction: insights into the Notch-mediated transcriptional switch.
  J Mol Biol, 365, 577-589.  
17157496 R.A.Kovall (2007).
Structures of CSL, Notch and Mastermind proteins: piecing together an active transcription complex.
  Curr Opin Struct Biol, 17, 117-127.  
16530044 Y.Nam, P.Sliz, L.Song, J.C.Aster, and S.C.Blacklow (2006).
Structural basis for cooperativity in recruitment of MAML coactivators to Notch transcription complexes.
  Cell, 124, 973-983.
PDB codes: 2f8x 2f8y
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 codes are shown on the right.

 

spacer
spacer