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PDBsum entry 1egf
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Growth factor
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PDB id
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1egf
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Contents |
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* Residue conservation analysis
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DOI no:
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Biochemistry
31:236-249
(1992)
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PubMed id:
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Solution structure of murine epidermal growth factor determined by NMR spectroscopy and refined by energy minimization with restraints.
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G.T.Montelione,
K.Wüthrich,
A.W.Burgess,
E.C.Nice,
G.Wagner,
K.D.Gibson,
H.A.Scheraga.
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ABSTRACT
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The solution structure of murine epidermal growth factor (mEGF) at pH 3.1 and a
temperature of 28 degrees C has been determined from NMR data, using distance
geometry calculations and restrained energy minimization. The structure
determination is based on 730 conformational constraints derived from NMR data,
including 644 NOE-derived upper bound distance constraints, constraints on the
ranges of 32 dihedral angles based on measurements of vicinal coupling
constants, and 54 upper and lower bound constraints associated with nine
hydrogen bonds and the three disulfide bonds. The distance geometry
interpretation of the NMR data is based on previously published
sequence-specific 1H resonance assignments [Montelione et al. (1988)
Biochemistry 27, 2235-2243], supplemented here with individual assignments for
some side-chain amide, methylene, and isopropyl methyl protons. The molecular
architecture of mEGF is the same as that described previously [Montelione et al.
(1987) Proc. Natl. Acad. Sci. U.S.A. 84, 5226-5230], but the structure is
overall more precisely determined by a more extensive set of NMR constraints.
Analysis of proton NMR line widths, amide proton exchange rates, and side-chain
3J(H alpha-H beta) coupling constants provides evidence for internal motion in
several regions of the mEGF molecule. Because mEGF is one member of a large
family of homologous growth factors and protein domains for which X-ray crystal
structures are not yet available, the atomic coordinates resulting from the
present structure refinement (which we have deposited in the Brookhaven Protein
Data Bank) are important data for understanding the structures of EGF-like
proteins and for further detailed comparisons of these structures with mEGF.
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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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C.Alemdaroğlu,
Z.Degim,
N.Celebi,
M.Sengezer,
M.Alömeroglu,
and
A.Nacar
(2008).
Investigation of epidermal growth factor containing liposome formulation effects on burn wound healing.
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J Biomed Mater Res A,
85,
271-283.
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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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N.Powers,
and
J.H.Jensen
(2006).
Chemically accurate protein structures: validation of protein NMR structures by comparison of measured and predicted pKa values.
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J Biomol NMR,
35,
39-51.
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H.Li,
A.D.Robertson,
and
J.H.Jensen
(2005).
Very fast empirical prediction and rationalization of protein pKa values.
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Proteins,
61,
704-721.
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H.S.Cho,
and
D.J.Leahy
(2002).
Structure of the extracellular region of HER3 reveals an interdomain tether.
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Science,
297,
1330-1333.
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PDB code:
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J.H.Kim,
K.Saito,
and
S.Yokoyama
(2002).
Chimeric receptor analyses of the interactions of the ectodomains of ErbB-1 with epidermal growth factor and of those of ErbB-4 with neuregulin.
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Eur J Biochem,
269,
2323-2329.
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N.E.Robinson,
and
A.B.Robinson
(2001).
Prediction of protein deamidation rates from primary and three-dimensional structure.
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Proc Natl Acad Sci U S A,
98,
4367-4372.
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S.G.Chamberlin,
L.Brennan,
S.M.Puddicombe,
D.E.Davies,
and
D.L.Turner
(2001).
Solution structure of the mEGF/TGFalpha44-50 chimeric growth factor.
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Eur J Biochem,
268,
6247-6255.
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PDB code:
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B.A.Sampoli Benitez,
and
E.A.Komives
(2000).
Disulfide bond plasticity in epidermal growth factor.
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Proteins,
40,
168-174.
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D.Tolkatchev,
and
F.Ni
(1998).
Calcium binding properties of an epidermal growth factor-like domain from human thrombomodulin.
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Biochemistry,
37,
9091-9100.
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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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M.Lohmeyer,
P.M.Harrison,
S.Kannan,
M.DeSantis,
N.J.O'Reilly,
M.J.Sternberg,
D.S.Salomon,
and
W.J.Gullick
(1997).
Chemical synthesis, structural modeling, and biological activity of the epidermal growth factor-like domain of human cripto.
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Biochemistry,
36,
3837-3845.
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A.E.Summerfield,
A.K.Hudnall,
T.J.Lukas,
C.A.Guyer,
and
J.V.Staros
(1996).
Identification of residues of the epidermal growth factor receptor proximal to residue 45 of bound epidermal growth factor.
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J Biol Chem,
271,
19656-19659.
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C.E.White,
M.J.Hunter,
D.P.Meininger,
S.Garrod,
and
E.A.Komives
(1996).
The fifth epidermal growth factor-like domain of thrombomodulin does not have an epidermal growth factor-like disulfide bonding pattern.
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Proc Natl Acad Sci U S A,
93,
10177-10182.
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J.W.Slootstra,
W.C.Puijk,
G.J.Ligtvoet,
J.P.Langeveld,
and
R.H.Meloen
(1996).
Structural aspects of antibody-antigen interaction revealed through small random peptide libraries.
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Mol Divers,
1,
87-96.
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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.Hrabal,
Z.Chen,
S.James,
H.P.Bennett,
and
F.Ni
(1996).
The hairpin stack fold, a novel protein architecture for a new family of protein growth factors.
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Nat Struct Biol,
3,
747-752.
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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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C.C.Lester,
B.Wang,
R.Wu,
and
H.A.Scheraga
(1995).
Structure-function studies of mEGF: probing the type I beta-turn between residues 25 and 26.
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J Protein Chem,
14,
753-762.
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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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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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G.Wagner,
and
D.F.Wyss
(1994).
Cell surface adhesion receptors.
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Curr Opin Struct Biol,
4,
841-851.
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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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M.S.Johnson,
N.Srinivasan,
R.Sowdhamini,
and
T.L.Blundell
(1994).
Knowledge-based protein modeling.
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Crit Rev Biochem Mol Biol,
29,
1.
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P.G.Gettins,
and
B.C.Crews
(1994).
Binding of epidermal growth factor to human alpha 2-macroglobulin. Significance for cytokine alpha 2-macroglobulin interactions.
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Ann N Y Acad Sci,
737,
383-398.
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B.Bax,
M.Blaber,
G.Ferguson,
M.J.Sternberg,
and
P.H.Walls
(1993).
Prediction of the three-dimensional structures of the nerve growth factor and epidermal growth factor binding proteins (kallikreins) and an hypothetical structure of the high molecular weight complex of epidermal growth factor with its binding protein.
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Protein Sci,
2,
1229-1241.
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J.Gallay,
M.Vincent,
I.M.de la Sierra,
J.Alvarez,
R.Ubieta,
J.Madrazo,
and
G.Padron
(1993).
Protein flexibility and aggregation state of human epidermal growth factor. A time-resolved fluorescence study of the native protein and engineered single-tryptophan mutants.
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Eur J Biochem,
211,
213-219.
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T.Ikura,
and
N.Go
(1993).
Normal mode analysis of mouse epidermal growth factor: characterization of the harmonic motion.
|
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Proteins,
16,
423-436.
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W.J.Chazin
(1992).
NMR structures and methodology.
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Curr Opin Biotechnol,
3,
326-332.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
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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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