scholarly journals Structure and Properties of the C-terminal Domain of Insulin-like Growth Factor-binding Protein-1 Isolated from Human Amniotic Fluid

2005 ◽  
Vol 280 (33) ◽  
pp. 29812-29819 ◽  
Author(s):  
Alberto Sala ◽  
Stefano Capaldi ◽  
Monica Campagnoli ◽  
Beniamino Faggion ◽  
Sara Labò ◽  
...  
Keyword(s):  
Growth Factor ◽  
Amniotic Fluid ◽  
Binding Protein ◽  
Insulin Like Growth Factor ◽  
Structure And Properties ◽  
Human Amniotic Fluid ◽  
Factor Binding ◽  
Terminal Domain

Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain

Biochimie ◽  
2012 ◽  
Vol 94 (3) ◽  
pp. 608-616 ◽  
Author(s):  
Charles A. Galea ◽  
Mehdi Mobli ◽  
Kerrie A. McNeil ◽  
Terrence D. Mulhern ◽  
John C. Wallace ◽  
...  
Keyword(s):  
Growth Factor ◽  
Structural Characterization ◽  
Binding Protein ◽  
Insulin Like Growth Factor ◽  
Nmr Analysis ◽  
Factor Binding ◽  
Terminal Domain

Fragmented Forms of Insulin-Like Growth Factor Binding Protein-1 in Amniotic Fluid of Patients With Preterm Labor and Intact Membranes

2011 ◽  
Vol 18 (9) ◽  
pp. 842-849 ◽  
Author(s):  
JoonHo Lee ◽  
Seung Mi Lee ◽  
Kyung Joon Oh ◽  
Chan-Wook Park ◽  
Jong Kwan Jun ◽  
...  
Keyword(s):  
Growth Factor ◽  
Amniotic Fluid ◽  
Preterm Labor ◽  
Binding Protein ◽  
Insulin Like Growth Factor ◽  
Factor Binding

scholarly journals Ligand-binding characteristics of recombinant amino- and carboxyl-terminal fragments of human insulin-like growth factor-binding protein-3

2001 ◽  
Vol 169 (1) ◽  
pp. 123-133 ◽  
Author(s):  
M Galanis ◽  
SM Firth ◽  
J Bond ◽  
A Nathanielsz ◽  
AA Kortt ◽  
...  
Keyword(s):  
Growth Factor ◽  
Binding Protein ◽  
Insulin Like Growth Factor ◽  
Factor Binding ◽  
Amino Terminal ◽  
Terminal Domain ◽  
Igf I ◽  
Igf Binding ◽  
Carboxyl Terminal ◽  
Igfbp 3

Insulin-like growth factor-binding protein-3 (IGFBP-3) is a member of a family of structurally conserved proteins (IGFBP-1 to -6) which act as carriers and regulators of the mitogenic peptide hormones IGF-I and IGF-II. Members of the IGFBP family share conserved cysteine-rich amino- and carboxyl-terminal regions. The amino-terminal domain of these proteins is recognised to contain an IGF-binding determinant, but evidence to support a binding site in the carboxyl-terminal region of the protein is less rigorous. To further investigate this, we have synthesised both the amino-terminal (residues 1-88; N-88) and carboxyl-terminal (residues 165-264; C-165) domains of human IGFBP-3 in bacteria, as fusion proteins with a carboxyl-terminal FLAG peptide. Although only C-165 showed binding to IGF-I and -II by solution-binding assays, both N-88 and C-165 demonstrated binding to IGF-I and -II by biosensor analysis albeit with reduced affinities compared with full-length IGFBP-3. Only the carboxyl-terminal fragment (C-165) was able to form hetero-trimeric complexes with IGF-I and the acid-labile subunit (ALS). We conclude that the carboxyl-terminal domain of IGFBP-3 contains an IGF-binding determinant and can form ternary complexes with ALS.

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