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PDBsum entry 3fub

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protein ligands Protein-protein interface(s) links
Hormone PDB id
3fub
Jmol
Contents
Protein chains
199 a.a. *
92 a.a. *
103 a.a. *
Ligands
EDO ×3
NAG
SO4
NAG-NAG
Waters ×167
* Residue conservation analysis
PDB id:
3fub
Name: Hormone
Title: Crystal structure of gdnf-gfralpha1 complex
Structure: Gdnf family receptor alpha-1. Chain: a, c. Fragment: sequence database residues 145-425. Synonym: gfr-alpha-1, gdnf receptor alpha, gdnfr-alpha, tgf related neurotrophic factor receptor 1, ret ligand 1. Glial cell line-derived neurotrophic factor. Chain: b, d. Synonym: astrocyte-derived trophic factor, atf, hgdnf. Engineered: yes
Source: Rattus norvegicus. Rat. Organism_taxid: 10116. Homo sapiens. Human. Organism_taxid: 9606. Gene: gdnf. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108.
Resolution:
2.35Å     R-factor:   0.228     R-free:   0.280
Authors: Parkash V.,Goldman A.
Key ref: V.Parkash and A.Goldman (2009). Comparison of GFL-GFRalpha complexes: further evidence relating GFL bend angle to RET signalling. Acta Crystallogr Sect F Struct Biol Cryst Commun, 65, 551-558. PubMed id: 19478429
Date:
14-Jan-09     Release date:   02-Jun-09    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q62997  (GFRA1_RAT) -  GDNF family receptor alpha-1
Seq:
Struc:
468 a.a.
199 a.a.
Protein chain
Pfam   ArchSchema ?
P39905  (GDNF_HUMAN) -  Glial cell line-derived neurotrophic factor
Seq:
Struc:
211 a.a.
92 a.a.
Protein chain
Pfam   ArchSchema ?
P39905  (GDNF_HUMAN) -  Glial cell line-derived neurotrophic factor
Seq:
Struc:
211 a.a.
103 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biochemical function     receptor activity     2 terms  

 

 
Acta Crystallogr Sect F Struct Biol Cryst Commun 65:551-558 (2009)
PubMed id: 19478429  
 
 
Comparison of GFL-GFRalpha complexes: further evidence relating GFL bend angle to RET signalling.
V.Parkash, A.Goldman.
 
  ABSTRACT  
 
Glial cell line-derived neurotrophic factor (GDNF) activates the receptor tyrosine kinase RET by binding to the GDNF-family receptor alpha1 (GFRalpha1) and forming the GDNF(2)-GFRalpha1(2)-RET(2) heterohexamer complex. A previous crystal structure of the GDNF(2)-GFRalpha1(2) complex (PDB code 2v5e) suggested that differences in signalling in GDNF-family ligand (GFL) complexes might arise from differences in the bend angle between the two monomers in the GFL homodimer. Here, a 2.35 A resolution structure of the GDNF(2)-GFRalpha1(2) complex crystallized with new cell dimensions is reported. The structure was refined to a final R factor of 22.5% (R(free) = 28%). The structures of both biological tetrameric complexes in the asymmetric unit are very similar to 2v5e and different from the artemin-GFRalpha3 structure, even though there is a small change in the structure of the GDNF. By comparison of all known GDNF and artemin structures, it is concluded that GDNF is more bent and more flexible than artemin and that this may be related to RET signalling. Comparisons also suggest that the differences between artemin and GDNF arise from the increased curvature of the artemin ;fingers', which both increases the buried surface area in the monomer-monomer interface and changes the intermonomer bend angle. From sequence comparison, it is suggested that neuturin (the second GFL) adopts an artemin-like conformation, while persephin has a different conformation to the other three.