spacer
spacer

PDBsum entry 5fm9

Go to PDB code: 
protein metals links
Transcription PDB id
5fm9

 

 

 

 

Loading ...

 
JSmol PyMol  
Contents
Protein chain
154 a.a.
Metals
_CA ×2
Waters ×6
PDB id:
5fm9
Name: Transcription
Title: Human notch 1, egf 4-7
Structure: Neurogenic locus notch homolog protein 1. Chain: a. Fragment: egf domains 4-7, unp residues 140-294. Synonym: notch 1, hn1, translocation-associated notch protein tan-1, notch 1 extracellular truncation, next, notch 1 intracellular domain, nicd. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Resolution:
2.92Å     R-factor:   0.214     R-free:   0.237
Authors: P.C.Weisshuhn,D.Sheppard,P.Taylor,P.Whiteman,S.M.Lea,P.A.Handford, C.Redfield
Key ref: P.C.Weisshuhn et al. (2016). Non-Linear and Flexible Regions of the Human Notch1 Extracellular Domain Revealed by High-Resolution Structural Studies. Structure, 24, 555-566. PubMed id: 26996961 DOI: 10.1016/j.str.2016.02.010
Date:
02-Nov-15     Release date:   20-Apr-16    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P46531  (NOTC1_HUMAN) -  Neurogenic locus notch homolog protein 1 from Homo sapiens
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
 
Seq:
Struc:
2555 a.a.
154 a.a.
Key:    PfamA domain  Secondary structure

 

 
DOI no: 10.1016/j.str.2016.02.010 Structure 24:555-566 (2016)
PubMed id: 26996961  
 
 
Non-Linear and Flexible Regions of the Human Notch1 Extracellular Domain Revealed by High-Resolution Structural Studies.
P.C.Weisshuhn, D.Sheppard, P.Taylor, P.Whiteman, S.M.Lea, P.A.Handford, C.Redfield.
 
  ABSTRACT  
 
The Notch receptor is a key component of a core metazoan signaling pathway activated by Delta/Serrate/Lag-2 ligands expressed on an adjacent cell. This results in a short-range signal with profound effects on cell-fate determination, cell proliferation, and cell death. Key to understanding receptor function is structural knowledge of the large extracellular portion of Notch which contains multiple repeats of epidermal growth factor (EGF)-like domains. Here we investigate the EGF4-13 region of human Notch1 (hN1) using a multidisciplinary approach. Ca(2+)-binding measurements, X-ray crystallography, {(1)H}-(15)N heteronuclear nuclear Overhauser effects, and residual dipolar couplings support a non-linear organization for the EGF4-13 region with a rigid, bent conformation for EGF4-7 and a single flexible linkage between EGF9 and EGF10. These data allow us to construct an informed model for EGF10-13 which, in conjunction with comparative binding studies, demonstrates that EGF10 has an important role in determining Notch receptor sensitivity to Dll-4.
 

 

spacer

spacer