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PDBsum entry 2tgf
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Growth factor
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PDB id
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2tgf
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Contents |
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* Residue conservation analysis
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Eur J Biochem
198:555-562
(1991)
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PubMed id:
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The solution structure of human transforming growth factor alpha.
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T.S.Harvey,
A.J.Wilkinson,
M.J.Tappin,
R.M.Cooke,
I.D.Campbell.
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ABSTRACT
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The solution structure of transforming growth factor alpha has been determined
by a combination of high-resolution 1H-nuclear magnetic resonance and distance
geometry and restrained molecular dynamics. The 382 restraints derived from the
NMR experiments were used to calculate many distance geometry structures, which
were then refined by restrained molecular mechanics. Five of these structures
were further refined using a variety of methods. Comparison of independently
measured parameters, such as calculated hydrogen bonding patterns and
experimental amide exchange rates, have been used to evaluate the accuracy of
the structures. Also, possible mechanisms to explain the pH-dependent
conformational interconversion observed are suggested. Finally comparisons
between this work and others on this topic have been made.
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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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K.Nagata
(2010).
Studies of the structure-activity relationships of peptides and proteins involved in growth and development based on their three-dimensional structures.
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Biosci Biotechnol Biochem,
74,
462-470.
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Q.Guo,
M.Manolopoulou,
Y.Bian,
A.B.Schilling,
and
W.J.Tang
(2010).
Molecular basis for the recognition and cleavages of IGF-II, TGF-alpha, and amylin by human insulin-degrading enzyme.
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J Mol Biol,
395,
430-443.
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PDB codes:
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I.Iloro,
D.Narváez,
N.Guillén,
C.M.Camacho,
L.Guillén,
E.Cora,
and
B.Pastrana-Ríos
(2008).
The kinetics of the hydrogen/deuterium exchange of epidermal growth factor receptor ligands.
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Biophys J,
94,
4041-4055.
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J.M.Kneller,
T.Ehlen,
J.P.Matisic,
D.Miller,
D.Van Niekerk,
W.L.Lam,
M.Marra,
R.Richards-Kortum,
M.Follen,
C.Macaulay,
and
S.J.Jones
(2007).
Using LongSAGE to Detect Biomarkers of Cervical Cancer Potentially Amenable to Optical Contrast Agent Labelling.
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Biomark Insights,
2,
447-461.
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M.Wingens,
T.Walma,
H.van Ingen,
C.Stortelers,
J.E.van Leeuwen,
E.J.van Zoelen,
and
G.W.Vuister
(2003).
Structural analysis of an epidermal growth factor/transforming growth factor-alpha chimera with unique ErbB binding specificity.
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J Biol Chem,
278,
39114-39123.
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PDB code:
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H.Ogiso,
R.Ishitani,
O.Nureki,
S.Fukai,
M.Yamanaka,
J.H.Kim,
K.Saito,
A.Sakamoto,
M.Inoue,
M.Shirouzu,
and
S.Yokoyama
(2002).
Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains.
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Cell,
110,
775-787.
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PDB code:
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M.Martin-Fernandez,
D.T.Clarke,
M.J.Tobin,
S.V.Jones,
and
G.R.Jones
(2002).
Preformed oligomeric epidermal growth factor receptors undergo an ectodomain structure change during signaling.
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Biophys J,
82,
2415-2427.
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T.P.Garrett,
N.M.McKern,
M.Lou,
T.C.Elleman,
T.E.Adams,
G.O.Lovrecz,
H.J.Zhu,
F.Walker,
M.J.Frenkel,
P.A.Hoyne,
R.N.Jorissen,
E.C.Nice,
A.W.Burgess,
and
C.W.Ward
(2002).
Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor alpha.
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Cell,
110,
763-773.
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PDB code:
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J.J.Chai,
M.Li,
B.R.Huang,
Y.Luo,
M.Luo,
R.C.Bi,
and
C.H.He
(2000).
Crystallization and preliminary X-ray diffraction studies of human epidermal growth factor.
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Acta Crystallogr D Biol Crystallogr,
56,
62-63.
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A.Muranyi,
B.E.Finn,
G.P.Gippert,
S.Forsén,
J.Stenflo,
and
T.Drakenberg
(1998).
Solution structure of the N-terminal EGF-like domain from human factor VII.
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Biochemistry,
37,
10605-10615.
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PDB code:
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B.Bersch,
J.F.Hernandez,
D.Marion,
and
G.J.Arlaud
(1998).
Solution structure of the epidermal growth factor (EGF)-like module of human complement protease C1r, an atypical member of the EGF family.
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Biochemistry,
37,
1204-1214.
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PDB code:
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C.McInnes,
J.Wang,
A.E.Al Moustafa,
C.Yansouni,
M.O'Connor-McCourt,
and
B.D.Sykes
(1998).
Structure-based minimization of transforming growth factor-alpha (TGF-alpha) through NMR analysis of the receptor-bound ligand. Design, solution structure, and activity of TGF-alpha 8-50.
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J Biol Chem,
273,
27357-27363.
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J.T.Jones,
M.D.Ballinger,
P.I.Pisacane,
J.A.Lofgren,
V.D.Fitzpatrick,
W.J.Fairbrother,
J.A.Wells,
and
M.X.Sliwkowski
(1998).
Binding interaction of the heregulinbeta egf domain with ErbB3 and ErbB4 receptors assessed by alanine scanning mutagenesis.
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J Biol Chem,
273,
11667-11674.
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K.J.Barnham,
A.M.Torres,
D.Alewood,
P.F.Alewood,
T.Domagala,
E.C.Nice,
and
R.S.Norton
(1998).
Role of the 6-20 disulfide bridge in the structure and activity of epidermal growth factor.
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Protein Sci,
7,
1738-1749.
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PDB code:
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C.McInnes,
and
B.D.Sykes
(1997).
Growth factor receptors: structure, mechanism, and drug discovery.
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Biopolymers,
43,
339-366.
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T.Mitamura,
T.Umata,
F.Nakano,
Y.Shishido,
T.Toyoda,
A.Itai,
H.Kimura,
and
E.Mekada
(1997).
Structure-function analysis of the diphtheria toxin receptor toxin binding site by site-directed mutagenesis.
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J Biol Chem,
272,
27084-27090.
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C.McInnes,
D.W.Hoyt,
R.N.Harkins,
R.N.Pagila,
M.T.Debanne,
M.O'Connor-McCourt,
and
B.D.Sykes
(1996).
NMR study of the transforming growth factor-alpha (TGF-alpha)-epidermal growth factor receptor complex. Visualization of human TGF-alpha binding determinants through nuclear Overhauser enhancement analysis.
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J Biol Chem,
271,
32204-32211.
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N.E.Jacobsen,
N.Abadi,
M.X.Sliwkowski,
D.Reilly,
N.J.Skelton,
and
W.J.Fairbrother
(1996).
High-resolution solution structure of the EGF-like domain of heregulin-alpha.
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Biochemistry,
35,
3402-3417.
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PDB codes:
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R.Tejero,
D.Bassolino-Klimas,
R.E.Bruccoleri,
and
G.T.Montelione
(1996).
Simulated annealing with restrained molecular dynamics using CONGEN: energy refinement of the NMR solution structures of epidermal and type-alpha transforming growth factors.
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Protein Sci,
5,
578-592.
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S.J.Freedman,
D.G.Sanford,
W.W.Bachovchin,
B.C.Furie,
J.D.Baleja,
and
B.Furie
(1996).
Structure and function of the epidermal growth factor domain of P-selectin.
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Biochemistry,
35,
13733-13744.
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PDB code:
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M.Adler,
M.H.Seto,
D.E.Nitecki,
J.H.Lin,
D.R.Light,
and
J.Morser
(1995).
The structure of a 19-residue fragment from the C-loop of the fourth epidermal growth factor-like domain of thrombomodulin.
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J Biol Chem,
270,
23366-23372.
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PDB code:
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M.J.Hunter,
and
E.A.Komives
(1995).
Thrombin-binding affinities of different disulfide-bonded isomers of the fifth EGF-like domain of thrombomodulin.
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Protein Sci,
4,
2129-2137.
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S.L.Lin,
and
R.Nussinov
(1995).
A disulphide-reinforced structural scaffold shared by small proteins with diverse functions.
|
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Nat Struct Biol,
2,
835-837.
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K.Nagata,
D.Kohda,
H.Hatanaka,
S.Ichikawa,
S.Matsuda,
T.Yamamoto,
A.Suzuki,
and
F.Inagaki
(1994).
Solution structure of the epidermal growth factor-like domain of heregulin-alpha, a ligand for p180erbB-4.
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EMBO J,
13,
3517-3523.
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PDB codes:
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R.J.Goodson,
M.V.Doyle,
S.E.Kaufman,
and
S.Rosenberg
(1994).
High-affinity urokinase receptor antagonists identified with bacteriophage peptide display.
|
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Proc Natl Acad Sci U S A,
91,
7129-7133.
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M.Baron,
D.G.Norman,
T.S.Harvey,
P.A.Handford,
M.Mayhew,
A.G.Tse,
G.G.Brownlee,
and
I.D.Campbell
(1992).
The three-dimensional structure of the first EGF-like module of human factor IX: comparison with EGF and TGF-alpha.
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Protein Sci,
1,
81-90.
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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
codes are
shown on the right.
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}
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