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91 a.a.
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96 a.a.
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91 a.a.
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95 a.a.
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* Residue conservation analysis
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PDB id:
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Growth factor
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Title:
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Glial cell-derived neurotrophic factor from rat
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Structure:
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Glial cell-derived neurotrophic factor. Chain: a, b, c, d. Synonym: gdnf. Engineered: yes
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Source:
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Rattus norvegicus. Norway rat. Organism_taxid: 10116. Organ: brain. Cell: glia. Expressed in: escherichia coli. Expression_system_taxid: 562
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Biol. unit:
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Tetramer (from
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Resolution:
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1.90Å
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R-factor:
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0.203
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R-free:
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0.235
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Authors:
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C.Eigenbrot,N.Gerber
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Key ref:
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C.Eigenbrot
and
N.Gerber
(1997).
X-ray structure of glial cell-derived neurotrophic factor at 1.9 A resolution and implications for receptor binding.
Nat Struct Biol,
4,
435-438.
PubMed id:
DOI:
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Date:
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25-Mar-97
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Release date:
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05-Jun-97
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PROCHECK
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Headers
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References
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Q07731
(GDNF_RAT) -
Glial cell line-derived neurotrophic factor
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Seq: Struc:
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211 a.a.
91 a.a.
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Q07731
(GDNF_RAT) -
Glial cell line-derived neurotrophic factor
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Seq: Struc:
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211 a.a.
96 a.a.
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Gene Ontology (GO) functional annotation
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Biochemical function
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growth factor activity
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1 term
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DOI no:
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Nat Struct Biol
4:435-438
(1997)
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PubMed id:
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X-ray structure of glial cell-derived neurotrophic factor at 1.9 A resolution and implications for receptor binding.
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C.Eigenbrot,
N.Gerber.
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ABSTRACT
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The crystal structure of glial cell-derived neurotrophic factor (GDNF) reveals
two independent copies of the dimer that differ significantly through a hinge
bending at the central, disulphide-rich region. GDNF is compared with other
members of the TGF-beta family, and potential receptor binding surfaces are
identified.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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B.S.Schmutzler,
S.Roy,
and
C.M.Hingtgen
(2009).
Glial cell line-derived neurotrophic factor family ligands enhance capsaicin-stimulated release of calcitonin gene-related peptide from sensory neurons.
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Neuroscience, 161,
148-156.
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K.Oh-hashi,
M.Ito,
T.Tanaka,
Y.Hirata,
and
K.Kiuchi
(2009).
Biosynthesis, processing, and secretion of glial cell line-derived neurotrophic factor in astroglial cells.
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Mol Cell Biochem, 323,
1-7.
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|
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V.Veverka,
A.J.Henry,
P.M.Slocombe,
A.Ventom,
B.Mulloy,
F.W.Muskett,
M.Muzylak,
K.Greenslade,
A.Moore,
L.Zhang,
J.Gong,
X.Qian,
C.Paszty,
R.J.Taylor,
M.K.Robinson,
and
M.D.Carr
(2009).
Characterization of the Structural Features and Interactions of Sclerostin: MOLECULAR INSIGHT INTO A KEY REGULATOR OF Wnt-MEDIATED BONE FORMATION.
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J Biol Chem, 284,
10890-10900.
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PDB code:
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V.Parkash,
V.M.Leppänen,
H.Virtanen,
J.M.Jurvansuu,
M.M.Bespalov,
Y.A.Sidorova,
P.Runeberg-Roos,
M.Saarma,
and
A.Goldman
(2008).
The Structure of the Glial Cell Line-derived Neurotrophic Factor-Coreceptor Complex: INSIGHTS INTO RET SIGNALING AND HEPARIN BINDING.
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J Biol Chem, 283,
35164-35172.
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PDB code:
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D.Sjöstrand,
J.Carlsson,
G.Paratcha,
B.Persson,
and
C.F.Ibáñez
(2007).
Disruption of the GDNF binding site in NCAM dissociates ligand binding and homophilic cell adhesion.
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J Biol Chem, 282,
12734-12740.
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F.Ledda,
G.Paratcha,
T.Sandoval-Guzmán,
and
C.F.Ibáñez
(2007).
GDNF and GFRalpha1 promote formation of neuronal synapses by ligand-induced cell adhesion.
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Nat Neurosci, 10,
293-300.
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O.Schueler-Furman,
E.Glick,
J.Segovia,
and
M.Linial
(2006).
Is GAS1 a co-receptor for the GDNF family of ligands?
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Trends Pharmacol Sci, 27,
72-77.
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S.Schlee,
P.Carmillo,
and
A.Whitty
(2006).
Quantitative analysis of the activation mechanism of the multicomponent growth-factor receptor Ret.
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Nat Chem Biol, 2,
636-644.
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X.Wang,
R.H.Baloh,
J.Milbrandt,
and
K.C.Garcia
(2006).
Structure of artemin complexed with its receptor GFRalpha3: convergent recognition of glial cell line-derived neurotrophic factors.
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Structure, 14,
1083-1092.
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PDB codes:
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L.M.Wang,
Q.Zhang,
Q.Zhang,
W.Zhu,
C.He,
C.L.Lu,
D.F.Ding,
and
Z.Y.Chen
(2004).
Identification of the key amino acids of glial cell line-derived neurotrophic factor family receptor alpha1 involved in its biological function.
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J Biol Chem, 279,
109-116.
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S.J.Lee
(2004).
Regulation of muscle mass by myostatin.
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Annu Rev Cell Dev Biol, 20,
61-86.
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V.M.Leppänen,
M.M.Bespalov,
P.Runeberg-Roos,
U.Puurand,
A.Merits,
M.Saarma,
and
A.Goldman
(2004).
The structure of GFRalpha1 domain 3 reveals new insights into GDNF binding and RET activation.
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EMBO J, 23,
1452-1462.
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PDB code:
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W.Sebald,
J.Nickel,
J.L.Zhang,
and
T.D.Mueller
(2004).
Molecular recognition in bone morphogenetic protein (BMP)/receptor interaction.
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Biol Chem, 385,
697-710.
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|
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S.Kjaer,
and
C.F.Ibáñez
(2003).
Identification of a surface for binding to the GDNF-GFR alpha 1 complex in the first cadherin-like domain of RET.
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J Biol Chem, 278,
47898-47904.
|
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T.B.Thompson,
T.K.Woodruff,
and
T.S.Jardetzky
(2003).
Structures of an ActRIIB:activin A complex reveal a novel binding mode for TGF-beta ligand:receptor interactions.
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EMBO J, 22,
1555-1566.
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PDB codes:
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P.J.Hart,
S.Deep,
A.B.Taylor,
Z.Shu,
C.S.Hinck,
and
A.P.Hinck
(2002).
Crystal structure of the human TbetaR2 ectodomain--TGF-beta3 complex.
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Nat Struct Biol, 9,
203-208.
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PDB code:
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P.K.Shah,
C.M.Buslje,
and
R.Sowdhamini
(2001).
Structural determinants of binding and specificity in transforming growth factor-receptor interactions.
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Proteins, 45,
408-420.
|
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|
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S.Manié,
M.Santoro,
A.Fusco,
and
M.Billaud
(2001).
The RET receptor: function in development and dysfunction in congenital malformation.
|
| |
Trends Genet, 17,
580-589.
|
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|
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|
|
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W.D.Fairlie,
P.K.Russell,
W.M.Wu,
A.G.Moore,
H.P.Zhang,
P.K.Brown,
A.R.Bauskin,
and
S.N.Breit
(2001).
Epitope mapping of the transforming growth factor-beta superfamily protein, macrophage inhibitory cytokine-1 (MIC-1): identification of at least five distinct epitope specificities.
|
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Biochemistry, 40,
65-73.
|
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|
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|
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J.A.Hongo,
S.P.Tsai,
B.Moffat,
K.A.Schroeder,
C.Jung,
A.Chuntharapai,
P.A.Lampe,
E.M.Johnson,
F.J.de Sauvage,
M.Armanini,
H.Phillips,
and
B.Devaux
(2000).
Characterization of novel neutralizing monoclonal antibodies specific to human neurturin.
|
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Hybridoma, 19,
303-315.
|
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|
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|
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M.G.Tansey,
R.H.Baloh,
J.Milbrandt,
and
E.M.Johnson
(2000).
GFRalpha-mediated localization of RET to lipid rafts is required for effective downstream signaling, differentiation, and neuronal survival.
|
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Neuron, 25,
611-623.
|
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|
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M.Saarma
(2000).
GDNF - a stranger in the TGF-beta superfamily?
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Eur J Biochem, 267,
6968-6971.
|
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|
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M.Tanaka,
S.Ito,
and
K.Kiuchi
(2000).
Novel alternative promoters of mouse glial cell line-derived neurotrophic factor gene.
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Biochim Biophys Acta, 1494,
63-74.
|
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|
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|
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R.H.Baloh,
M.G.Tansey,
E.M.Johnson,
and
J.Milbrandt
(2000).
Functional mapping of receptor specificity domains of glial cell line-derived neurotrophic factor (GDNF) family ligands and production of GFRalpha1 RET-specific agonists.
|
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J Biol Chem, 275,
3412-3420.
|
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C.J.Xian,
B.R.Huang,
and
X.F.Zhou
(1999).
Distribution of neurturin mRNA and immunoreactivity in the peripheral tissues of adult rats.
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Brain Res, 835,
247-258.
|
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|
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M.Saarma,
and
H.Sariola
(1999).
Other neurotrophic factors: glial cell line-derived neurotrophic factor (GDNF).
|
| |
Microsc Res Tech, 45,
292-302.
|
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S.Eketjäll,
M.Fainzilber,
J.Murray-Rust,
and
C.F.Ibáñez
(1999).
Distinct structural elements in GDNF mediate binding to GFRalpha1 and activation of the GFRalpha1-c-Ret receptor complex.
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| |
EMBO J, 18,
5901-5910.
|
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|
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|
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C.F.Ibáñez
(1998).
Emerging themes in structural biology of neurotrophic factors.
|
| |
Trends Neurosci, 21,
438-444.
|
 |
|
|
|
|
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J.Milbrandt,
F.J.de Sauvage,
T.J.Fahrner,
R.H.Baloh,
M.L.Leitner,
M.G.Tansey,
P.A.Lampe,
R.O.Heuckeroth,
P.T.Kotzbauer,
K.S.Simburger,
J.P.Golden,
J.A.Davies,
R.Vejsada,
A.C.Kato,
M.Hynes,
D.Sherman,
M.Nishimura,
L.C.Wang,
R.Vandlen,
B.Moffat,
R.D.Klein,
K.Poulsen,
C.Gray,
A.Garces,
and
E.M.Johnson
(1998).
Persephin, a novel neurotrophic factor related to GDNF and neurturin.
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Neuron, 20,
245-253.
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|
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K.Wartiovaara,
M.Salo,
and
H.Sariola
(1998).
Hirschsprung's disease genes and the development of the enteric nervous system.
|
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Ann Med, 30,
66-74.
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Y.A.Muller,
H.W.Christinger,
B.A.Keyt,
and
A.M.de Vos
(1997).
The crystal structure of vascular endothelial growth factor (VEGF) refined to 1.93 A resolution: multiple copy flexibility and receptor binding.
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Structure, 5,
1325-1338.
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PDB code:
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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.
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