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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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References listed in PDB file
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Key reference
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Title
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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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Authors
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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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Ref.
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Biochemistry, 1992,
31,
236-249.
[DOI no: ]
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PubMed id
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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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Secondary reference #1
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Title
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Sequence-Specific 1h nmr assignments and identification of slowly exchanging amide protons in murine epidermal growth factor.
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Authors
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G.T.Montelione,
K.Wüthrich,
H.A.Scheraga.
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Ref.
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Biochemistry, 1988,
27,
2235-2243.
[DOI no: ]
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PubMed id
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Secondary reference #2
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Title
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Solution structure of murine epidermal growth factor: determination of the polypeptide backbone chain-Fold by nuclear magnetic resonance and distance geometry.
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Authors
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G.T.Montelione,
K.Wüthrich,
E.C.Nice,
A.W.Burgess,
H.A.Scheraga.
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Ref.
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Proc Natl Acad Sci U S A, 1987,
84,
5226-5230.
[DOI no: ]
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PubMed id
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Secondary reference #3
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Title
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Identification of two anti-Parallel beta-Sheet conformations in the solution structure of murine epidermal growth factor by proton magnetic resonance.
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Authors
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G.T.Montelione,
K.Wüthrich,
E.C.Nice,
A.W.Burgess,
H.A.Scheraga.
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Ref.
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Proc Natl Acad Sci U S A, 1986,
83,
8594-8598.
[DOI no: ]
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PubMed id
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