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PDBsum entry 1yug
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Growth factor
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PDB id
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1yug
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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 human type-Alpha transforming growth factor determined by heteronuclear nmr spectroscopy and refined by energy minimization with restraints.
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Authors
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F.J.Moy,
Y.C.Li,
P.Rauenbuehler,
M.E.Winkler,
H.A.Scheraga,
G.T.Montelione.
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Ref.
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Biochemistry, 1993,
32,
7334-7353.
[DOI no: ]
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PubMed id
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Abstract
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Human type-alpha transforming growth factor (hTGF alpha) is a small mitogenic
protein containing 50 amino acids and 3 disulfide bonds. Homo- and heteronuclear
NMR spectra were used to determine nearly complete sequence-specific 1H and 15N
resonance assignments for hTGF alpha under three conditions: pH 6.5 and a
temperature of 10 degrees C, pH 6.5 and a temperature of 30 degrees C, and pH
3.5 and a temperature of 30 degrees C. The 15N-enriched samples of hTGF alpha
allowed determination of many 3J(HN-H alpha) vicinal coupling constants.
Solution structures of human type-alpha transforming growth factor (hTGF alpha)
at pH 6.5 and a temperature of 10 degrees C were determined from NMR data using
molecular structure generation calculations and restrained energy minimization.
These structures are based on 425 conformational constraints, including 357
NOE-derived upper-bound distance constraints, constraints on the ranges of 26
dihedral angles based on measurements of vicinal coupling constants, 42 upper-
and lower-bound constraints associated with 6 hydrogen bonds and 3 disulfide
bonds, and several stereospecific 1H resonance assignments. The overall
structure is similar to that described recently for hTGF alpha by other groups
[Kline et al. (1990) Biochemistry 29, 7805-7813; Harvey et al. (1991). Eur. J.
Biochem. 198, 555-562], but there are differences in some structural details.
The resonance frequencies, vicinal coupling constants, and NOEs form the basis
for comparisons of the solution structure of hTGF alpha at neutral and acidic
pH. At pH 3.5 the protein structure is partially disordered, with most of the
hydrogen-bonded backbone structure still intact. The hTGF alpha structure is
also compared with that of murine epidermal growth factor. Coordinates for the
set of hTGF alpha structures described in this paper have been deposited in the
Protein Data Bank.
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Secondary reference #1
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Title
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Crankshaft motions of the polypeptide backbone in molecular dynamics simulations of human type-Alpha transforming growth factor.
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Authors
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A.R.Fadel,
D.Q.Jin,
G.T.Montelione,
R.M.Levy.
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Ref.
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J Biomol Nmr, 1995,
6,
221-226.
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PubMed id
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Secondary reference #2
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Title
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Human type-Alpha transforming growth factor undergoes slow conformational exchange between multiple backbone conformations as characterized by nitrogen-15 relaxation measurements.
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Authors
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Y.C.Li,
G.T.Montelione.
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Ref.
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Biochemistry, 1995,
34,
2408-2423.
[DOI no: ]
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PubMed id
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Secondary reference #3
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Title
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Sequence-Specific 1h-Nmr assignments and identification of two small antiparallel beta-Sheets in the solution structure of recombinant human transforming growth factor alpha.
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Authors
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G.T.Montelione,
M.E.Winkler,
L.E.Burton,
E.Rinderknecht,
M.B.Sporn,
G.Wagner.
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Ref.
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Proc Natl Acad Sci U S A, 1989,
86,
1519-1523.
[DOI no: ]
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PubMed id
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