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PDBsum entry 1b9g
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Growth factor
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PDB id
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1b9g
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Contents |
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* Residue conservation analysis
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DOI no:
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Protein Sci
5:2193-2202
(1996)
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PubMed id:
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Solution structure of a mini IGF-1.
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E.De Wolf,
R.Gill,
S.Geddes,
J.Pitts,
A.Wollmer,
J.Grötzinger.
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ABSTRACT
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Mini insulin-like growth factor 1, an inactive insulin-like growth factor 1
mutant lacking the C region, was studied by 2D NMR spectroscopy. Resonances were
assigned for almost all protons of the 57 amino acid residues. The 3D structure
of the protein was determined by distance geometry methods. Three helical
segments; Ala 8-Cys 18, Gly 42-Phe 49, and Leu 54-Cys 61, were identified,
corresponding to those present in wild-type insulin-like growth factor 1 and in
single-chain insulin. Their relative orientation, however, was found to be
changed. This change is connected with a displacement of the Phe 23-Tyr 24-Phe
25-Asn 26 beta-strand-like segment, i.e., of aromatic side chains known to be
important for receptor binding. Thus, deletion of the C region of IGF-1 results
in a substantial tertiary structural rearrangement that accounts for the loss of
receptor affinity.
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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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Y.Sohma,
Q.X.Hua,
M.Liu,
N.B.Phillips,
S.Q.Hu,
J.Whittaker,
L.J.Whittaker,
A.Ng,
C.T.Roberts,
P.Arvan,
S.B.Kent,
and
M.A.Weiss
(2010).
Contribution of residue B5 to the folding and function of insulin and IGF-I: constraints and fine-tuning in the evolution of a protein family.
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J Biol Chem,
285,
5040-5055.
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G.Vardatsikos,
A.Sahu,
and
A.K.Srivastava
(2009).
The insulin-like growth factor family: molecular mechanisms, redox regulation, and clinical implications.
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Antioxid Redox Signal,
11,
1165-1190.
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A.Denley,
L.J.Cosgrove,
G.W.Booker,
J.C.Wallace,
and
B.E.Forbes
(2005).
Molecular interactions of the IGF system.
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Cytokine Growth Factor Rev,
16,
421-439.
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Z.Y.Guo,
L.Shen,
and
Y.M.Feng
(2002).
The different folding behavior of insulin and insulin-like growth factor 1 is mainly controlled by their B-chain/domain.
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Biochemistry,
41,
1556-1567.
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Z.Y.Guo,
L.Shen,
and
Y.M.Feng
(2002).
The different energetic state of the intra A-chain/domain disulfide of insulin and insulin-like growth factor 1 is mainly controlled by their B-chain/domain.
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Biochemistry,
41,
10585-10592.
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N.J.Skelton,
Y.M.Chen,
N.Dubree,
C.Quan,
D.Y.Jackson,
A.Cochran,
K.Zobel,
K.Deshayes,
M.Baca,
M.T.Pisabarro,
and
H.B.Lowman
(2001).
Structure-function analysis of a phage display-derived peptide that binds to insulin-like growth factor binding protein 1.
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Biochemistry,
40,
8487-8498.
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PDB codes:
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P.Barthe,
S.Rochette,
C.Vita,
and
C.Roumestand
(2000).
Synthesis and NMR solution structure of an alpha-helical hairpin stapled with two disulfide bridges.
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Protein Sci,
9,
942-955.
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PDB code:
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Y.Dubaquié,
and
H.B.Lowman
(1999).
Total alanine-scanning mutagenesis of insulin-like growth factor I (IGF-I) identifies differential binding epitopes for IGFBP-1 and IGFBP-3.
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Biochemistry,
38,
6386-6396.
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H.B.Lowman,
Y.M.Chen,
N.J.Skelton,
D.L.Mortensen,
E.E.Tomlinson,
M.D.Sadick,
I.C.Robinson,
and
R.G.Clark
(1998).
Molecular mimics of insulin-like growth factor 1 (IGF-1) for inhibiting IGF-1: IGF-binding protein interactions.
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Biochemistry,
37,
8870-8878.
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PDB codes:
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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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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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Links
