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Growth factor
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PDB id
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1bqt
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Contents |
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* Residue conservation analysis
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PDB id:
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Growth factor
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Title:
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Three-dimensional structure of human insulin-like growth factor-i (igf-i) determined by 1h-nmr and distance geometry, 6 structures
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Structure:
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Insulin-like growth factor-i. Chain: a. Synonym: somatomedin c. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli. Expression_system_taxid: 562
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NMR struc:
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6 models
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Authors:
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A.Sato,S.Nishimura,T.Ohkubo,Y.Kyogoku,S.Koyama,M.Kobayashi, T.Yasuda,Y.Kobayashi
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Key ref:
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A.Sato
et al.
(1993).
Three-dimensional structure of human insulin-like growth factor-I (IGF-I) determined by 1H-NMR and distance geometry.
Int J Pept Protein Res,
41,
433-440.
PubMed id:
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Date:
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18-Aug-98
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Release date:
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18-May-99
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PROCHECK
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Headers
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References
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P05019
(IGF1_HUMAN) -
Insulin-like growth factor I
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Seq:
Struc:
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195 a.a.
70 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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Gene Ontology (GO) functional annotation
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Cellular component
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extracellular region
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2 terms
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Biochemical function
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hormone activity
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2 terms
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Int J Pept Protein Res
41:433-440
(1993)
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PubMed id:
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Three-dimensional structure of human insulin-like growth factor-I (IGF-I) determined by 1H-NMR and distance geometry.
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A.Sato,
S.Nishimura,
T.Ohkubo,
Y.Kyogoku,
S.Koyama,
M.Kobayashi,
T.Yasuda,
Y.Kobayashi.
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ABSTRACT
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The three-dimensional structure of human insulin-like growth factor-I has been
determined through a combination of NMR measurements and distance geometry
calculations. A total of 320 interatomic distance constraints, including 12
related to the disulfide bridges, were used in these calculations. The resulting
structure is characterized by the presence of three helical rods corresponding
to the sequence regions, Ala8-Cys18, Gly42-Cys48 and Leu54-Cys61. Furthermore, a
turn structure and an extended structure exist in the Gly19-Gly22 and
Phe23-Asn26 regions, respectively. Neglecting the N- and C-termini, with their
expectedly high degree of mobility as well as a fluctuating C-domain, the
r.m.s.d. value is 1.9 A for backbone atoms. Those of the three alpha-helical
regions are 1.0, 0.9 and 0.8 A, respectively, 1.8 A being that for the total
backbone atoms participating in the formation of these three helices, showing
the good convergence of their spatial arrangements. The overall structure
obtained here shows that the human IGF-I molecule folds into a spatial structure
very similar to that of insulin in an aqueous solution.
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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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C.L.Alvino,
K.A.McNeil,
S.C.Ong,
C.Delaine,
G.W.Booker,
J.C.Wallace,
J.Whittaker,
and
B.E.Forbes
(2009).
A Novel Approach to Identify Two Distinct Receptor Binding Surfaces of Insulin-like Growth Factor II.
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J Biol Chem, 284,
7656-7664.
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E.E.Büllesbach,
M.A.Hass,
M.R.Jensen,
D.F.Hansen,
S.M.Kristensen,
C.Schwabe,
and
J.J.Led
(2008).
Solution structure of a conformationally restricted fully active derivative of the human relaxin-like factor.
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Biochemistry, 47,
13308-13317.
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PDB codes:
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L.Gauguin,
C.Delaine,
C.L.Alvino,
K.A.McNeil,
J.C.Wallace,
B.E.Forbes,
and
P.De Meyts
(2008).
Alanine scanning of a putative receptor binding surface of insulin-like growth factor-I.
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J Biol Chem, 283,
20821-20829.
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Q.X.Hua,
J.P.Mayer,
W.Jia,
J.Zhang,
and
M.A.Weiss
(2006).
The folding nucleus of the insulin superfamily: a flexible peptide model foreshadows the native state.
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J Biol Chem, 281,
28131-28142.
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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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S.Lien,
S.J.Milner,
L.D.Graham,
J.C.Wallace,
and
G.L.Francis
(2001).
Linkers for improved cleavage of fusion proteins with an engineered alpha-lytic protease.
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Biotechnol Bioeng, 74,
335-343.
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W.Zesławski,
H.G.Beisel,
M.Kamionka,
W.Kalus,
R.A.Engh,
R.Huber,
K.Lang,
and
T.A.Holak
(2001).
The interaction of insulin-like growth factor-I with the N-terminal domain of IGFBP-5.
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EMBO J, 20,
3638-3644.
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PDB code:
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G.Fullbright,
and
E.E.Büllesbach
(2000).
The receptor binding conformation of bombyxin is induced by alanine(B15).
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Biochemistry, 39,
9718-9724.
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L.G.Laajoki,
G.L.Francis,
J.C.Wallace,
J.A.Carver,
and
M.A.Keniry
(2000).
Solution structure and backbone dynamics of long-[Arg(3)]insulin-like growth factor-I.
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J Biol Chem, 275,
10009-10015.
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PDB code:
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J.B.Janosi,
P.A.Ramsland,
M.R.Mott,
S.M.Firth,
R.C.Baxter,
and
P.J.Delhanty
(1999).
The acid-labile subunit of the serum insulin-like growth factor-binding protein complexes. Structural determination by molecular modeling and electron microscopy.
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J Biol Chem, 274,
23328-23332.
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S.J.Milner,
J.A.Carver,
F.J.Ballard,
and
G.L.Francis
(1999).
Probing the disulfide folding pathway of insulin-like growth factor-I.
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Biotechnol Bioeng, 62,
693-703.
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G.D.Hobba,
A.Löthgren,
E.Holmberg,
B.E.Forbes,
G.L.Francis,
and
J.C.Wallace
(1998).
Alanine screening mutagenesis establishes tyrosine 60 of bovine insulin-like growth factor binding protein-2 as a determinant of insulin-like growth factor binding.
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J Biol Chem, 273,
19691-19698.
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M.Jansson,
G.Andersson,
M.Uhlén,
B.Nilsson,
and
J.Kördel
(1998).
The insulin-like growth factor (IGF)binding protein 1 binding epitope on IGF-I probed by heteronuclear NMR spectroscopy and mutational analysis.
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J Biol Chem, 273,
24701-24707.
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W.Engström,
A.Shokrai,
K.Otte,
M.Granérus,
A.Gessbo,
P.Bierke,
A.Madej,
M.Sjölund,
and
A.Ward
(1998).
Transcriptional regulation and biological significance of the insulin like growth factor II gene.
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Cell Prolif, 31,
173-189.
|
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|
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|
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C.McInnes,
and
B.D.Sykes
(1997).
Growth factor receptors: structure, mechanism, and drug discovery.
|
| |
Biopolymers, 43,
339-366.
|
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|
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|
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E.De Wolf,
R.Gill,
S.Geddes,
J.Pitts,
A.Wollmer,
and
J.Grötzinger
(1996).
Solution structure of a mini IGF-1.
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Protein Sci, 5,
2193-2202.
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PDB code:
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D.R.Hodgson,
F.E.May,
and
B.R.Westley
(1995).
Mutations at positions 11 and 60 of insulin-like growth factor 1 reveal differences between its interactions with the type I insulin-like-growth-factor receptor and the insulin receptor.
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Eur J Biochem, 233,
299-309.
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R.Kreisberg,
V.Buchner,
and
D.Arad
(1995).
Paired natural cysteine mutation mapping: aid to constraining models of protein tertiary structure.
|
| |
Protein Sci, 4,
2405-2410.
|
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|
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H.Terasawa,
D.Kohda,
H.Hatanaka,
K.Nagata,
N.Higashihashi,
H.Fujiwara,
K.Sakano,
and
F.Inagaki
(1994).
Solution structure of human insulin-like growth factor II; recognition sites for receptors and binding proteins.
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EMBO J, 13,
5590-5597.
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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
