spacer
spacer
Go to PDB code: 
protein ligands Protein-protein interface(s) links
Hormone/growth factor PDB-id
2ask
Biological unit* = asymmetric unit,
as shown
(*as deduced by PQS)
    Jmol     Help!  
Contents
Description
Header details
Header records
References
PROCHECK
Protein chains
101 a.a. *
Ligands
SO4 ×6
Waters ×212

* Residue conservation analysis
Tools
Image Generation
AstexViewer™@PDBe
Run PROCHECK
Clefts Calculation
  
PDB id: 2ask
Name: Hormone/growth factor
Title: Structure of human artemin

Structure:
Artemin. Chain: a, b. Engineered: yes

Source:
Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562.

Biological unit:
Dimer (from PQS)

UniProt:
Chains A, B: Q5T4W7 (ARTN_HUMAN)
Pfam   ArchSchema ?
Seq: 220 a.a.
Struc: 101 a.a.
Key:    PfamA domain
 Secondary structure  CATH domain

Resolution:
1.55Å

R-factor:
0.231

R-free:
0.255

Authors:
L.Silvian,P.Jin,P.Carmillo,P.A.Boriack-Sjodin,C.Pelletier, M.Rushe,B.J.Gong,D.Sah,B.Pepinsky,A.Rossomando

Key ref:
L.Silvian et al. (2006). Artemin crystal structure reveals insights into heparan sulfate binding.. Biochemistry, 45, 6801-6812. [PubMed id: 16734417] [DOI: 10.1021/bi060035x]

Date:
23-Aug-05

Release date:
13-Jun-06
Quick_links
RCSB
PDBe
SRS
MMDB
JenaLib
OCA
PDBWiki
Proteopedia
CATH
SCOP
FSSP
HSSP
PDBSWS
PQS
ProSAT
Whatcheck
EDS
Procheck
Go to PROCHECK summary
Clefts
Clefts
Surface
RasMol surface
spacer
spacer

 
    Key reference    
 
 
DOI no: 10.1021/bi060035x Biochemistry 45:6801-6812 (2006)
PubMed id: 16734417  
 
 
Artemin crystal structure reveals insights into heparan sulfate binding.
L.Silvian, P.Jin, P.Carmillo, P.A.Boriack-Sjodin, C.Pelletier, M.Rushe, B.Gong, D.Sah, B.Pepinsky, A.Rossomando.
 
  ABSTRACT  
 
Artemin (ART) promotes the growth of developing peripheral neurons by signaling through a multicomponent receptor complex comprised of a transmembrane tyrosine kinase receptor (cRET) and a specific glycosylphosphatidylinositol-linked co-receptor (GFRalpha3). Glial cell line-derived neurotrophic factor (GDNF) signals through a similar ternary complex but requires heparan sulfate proteoglycans (HSPGs) for full activity. HSPG has not been demonstrated as a requirement for ART signaling. We crystallized ART in the presence of sulfate and solved its structure by isomorphous replacement. The structure reveals ordered sulfate anions bound to arginine residues in the pre-helix and amino-terminal regions that were organized in a triad arrangement characteristic of heparan sulfate. Three residues in the pre-helix were singly or triply substituted with glutamic acid, and the resulting proteins were shown to have reduced heparin-binding affinity that is partly reflected in their ability to activate cRET. This study suggests that ART binds HSPGs and identifies residues that may be involved in HSPG binding.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
18465825 M.D.Wood, G.H.Borschel, and S.E.Sakiyama-Elbert (2009).
Controlled release of glial-derived neurotrophic factor from fibrin matrices containing an affinity-based delivery system.
  J Biomed Mater Res A, 89, 909-918.  
19090915 N.S.Gandhi, and R.L.Mancera (2008).
The structure of glycosaminoglycans and their interactions with proteins.
  Chem Biol Drug Des, 72, 455-482.  
17013378 S.Schlee, P.Carmillo, and A.Whitty (2006).
Quantitative analysis of the activation mechanism of the multicomponent growth-factor receptor Ret.
  Nat Chem Biol, 2, 636-644.  
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.