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PDBsum entry 1gk5
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Growth factor
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PDB id
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1gk5
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Contents |
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* Residue conservation analysis
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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 the megf/tgfalpha44-50 chimeric growth factor.
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Authors
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S.G.Chamberlin,
L.Brennan,
S.M.Puddicombe,
D.E.Davies,
D.L.Turner.
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Ref.
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Eur J Biochem, 2001,
268,
6247-6255.
[DOI no: ]
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PubMed id
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Abstract
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The solution structure of the growth factor chimera mEGF/TGFalpha44-50 has been
determined using an extended version of the dyana procedure for calculating
structures from NMR data. The backbone fold and preferred orientation of the
domains of the chimera are similar to those found in previous studies of EGF
structures, and several H-bonds used as input constraints in those studies were
found independently in the chimera. This shows that the modified activity of the
chimera does not result from a major structural change. However, the improved
precision of the structure presented here allows the origin of some unusual
chemical shifts found in all of these compounds to be explained, as well as the
results obtained from some site-specific mutants. Further studies of the
properties of this chimeric growth factor should help to elucidate the
mechanism(s) of hetero- and homodimerization of the c-erbB receptors.
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Figure 1.
Fig. 1 NMR Data. Top: the number of meaningful NOE-derived
constraints for each residue used in the calculations. White
represents intraresidual constraints (  i = 0), light
grey sequential ( i = 1), grey
and black represent medium ( i < 5) and
long-range ( i  5) constraints.
Both lower and upper volume limits are included. Bottom: average
rmsd (Å) for the backbone (  ) and heavy
atoms (  ) with
respect to the mean structure. The superimposition was performed
for residues 5–47.
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Figure 2.
Fig. 2 Stereo view of the of the 10 best chimera
structures, superimposed using the backbones of residues 5–47.
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The above figures are
reprinted
by permission from the Federation of European Biochemical Societies:
Eur J Biochem
(2001,
268,
6247-6255)
copyright 2001.
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Secondary reference #1
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Title
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The interaction of an epidermal growth factor/transforming growth factor alpha tail chimera with the human epidermal growth factor receptor reveals unexpected complexities.
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Authors
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S.M.Puddicombe,
L.Wood,
S.G.Chamberlin,
D.E.Davies.
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Ref.
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J Biol Chem, 1996,
271,
30392-30397.
[DOI no: ]
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PubMed id
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Figure 1.
Fig. 1. Diagrammatic representation of mEGF and the mEGF/TGF-
 [44-50]
chimera. In the chimera the carboxyl-terminal 7 residues from
TGF- are shown
in boldface.
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Figure 4.
Fig. 4. Comparison of the receptor binding and mitogenic
activities of TGF- (  ), mEGF (
 circle ),
and mEGF/TGF- [44-50] (
 ) for
chicken embryo fibroblasts. In panel A, relative receptor
binding affinities were measured in competitive binding assays
using 125I-labeled hEGF on intact CEFs. In panel B, mitogenic
activities were determined by measuring incorporation of the
thymidine analog [125I]dUdR into DNA of CEFs as described under
"Experimental Procedures." Data shown are representative of two
individual experiments.
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The above figures are
reproduced from the cited reference
with permission from the ASBMB
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