Related ArticlesThe insulin-like growth factor (IGF)binding protein 1 binding epitope on IGF-I probed by heteronuclear NMR spectroscopy and mutational analysis.
J Biol Chem. 1998 Sep 18;273(38):24701-7
Authors: Jansson M, Andersson G, Uhlén M, Nilsson B, Kördel J
NMR spectroscopy studies and biosensor interaction analysis of native and site-directed mutants of insulin-like growth factor I (IGF-I) was applied to identify the involvement of individual residues in IGF-I binding to IGF-binding protein 1 (IGFBP-1). Backbone NMR chemical shifts were found to be affected by IGFBP-1 binding in the following residues: Pro2, Glu3, Cys6, Gly7, Gly19, Pro28-Gly30, Gly32, Arg36, Arg37, Gln40-Gly42, Pro63, Lys65, Pro66, and Lys68-Ala70. Three IGF-I arginine side chains were identified by NMR to participate in IGFBP-1 binding. All IGF-I arginine residues were replaced by alanines, using site-directed mutagenesis, in four single substituted variants, IGF-I(R21A), IGF-I(R50A), IGF-I(R55A), and IGF-I(R56A), and one double replacement mutant, IGF-I(R36A/R37A). Biosensor interaction analysis binding studies demonstrate the involvement of Arg36-Arg37 and Arg50 in IGFBP-1 binding, while experiments with the IGF-I receptor implicate Arg21, Arg36-Arg37, and Arg56 as part of the receptor binding epitope. These overlapping binding surfaces explain why IGF-I receptor and IGFBP-1 binding to IGF-I is competitive. The C terminus of free, but not IGFBP-1-bound, IGF-I is found to exist in two distinct, NMR-detectable conformations at 30 degreesC. One possible explanation for this structural heterogeneity could be cis-trans isomerization of the Cys6-Cys48 disulfide bond.
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Biochimie. 2011 Sep 22;
Authors: Galea CA, Mobli M, McNeil KA, Mulhern TD, Wallace JC, King GF, Forbes BE, Norton RS
Abstract
The insulin-like growth factor binding proteins are a family of six proteins (IGFBP-1 to 6) that bind insulin-like growth factors-I and -II (IGF-I/II) with high affinity. In addition...
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Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Biochimie. 2011 Sep 22;
Authors: Galea CA, Mobli M, McNeil KA, Mulhern TD, Wallace JC, King GF, Forbes BE, Norton RS
Abstract
The insulin-like growth factor binding proteins are a family of six proteins (IGFBP-1 to 6) that bind insulin-like growth factors-I and -II (IGF-I/II) with high affinity. In...
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09-30-2011 05:59 AM
Calcium binding environments probed by (43)Ca NMR spectroscopy.
Calcium binding environments probed by (43)Ca NMR spectroscopy.
Calcium binding environments probed by (43)Ca NMR spectroscopy.
Dalton Trans. 2010 Oct 7;39(37):8593-602
Authors: Bryce DL
Calcium is an important component of materials, metalloproteins, minerals, glasses, and small inorganic and organic complexes. However, NMR spectroscopy of the quadrupolar (43)Ca nuclide remains difficult primarily due to its low natural abundance and low resonance frequency. In this Perspective, experimental challenges and recent successes in the field are...
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[NMR paper] NMR assignments of the cold-shock protein ribosome-binding factor A (RbfA) from Therm
NMR assignments of the cold-shock protein ribosome-binding factor A (RbfA) from Thermotoga maritima.
Related Articles NMR assignments of the cold-shock protein ribosome-binding factor A (RbfA) from Thermotoga maritima.
J Biomol NMR. 2005 Jan;31(1):73-4
Authors: Grimm SK, Wöhnert J
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[NMR paper] NMR-based determination of the binding epitope and conformational analysis of MUC-1 g
NMR-based determination of the binding epitope and conformational analysis of MUC-1 glycopeptides and peptides bound to the breast cancer-selective monoclonal antibody SM3.
Related Articles NMR-based determination of the binding epitope and conformational analysis of MUC-1 glycopeptides and peptides bound to the breast cancer-selective monoclonal antibody SM3.
Eur J Biochem. 2002 Mar;269(5):1444-55
Authors: Möller H, Serttas N, Paulsen H, Burchell JM, Taylor-Papadimitriou J,
Mucin glycoproteins on breast cancer cells carry shortened...
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[NMR paper] NMR 15N relaxation of the insulin-like growth factor (IGF)-binding domain of IGF bind
NMR 15N relaxation of the insulin-like growth factor (IGF)-binding domain of IGF binding protein-5 (IGFBP-5) determined free in solution and in complex with IGF-II.
Related Articles NMR 15N relaxation of the insulin-like growth factor (IGF)-binding domain of IGF binding protein-5 (IGFBP-5) determined free in solution and in complex with IGF-II.
Eur J Biochem. 2001 Feb;268(4):1058-65
Authors: Renner C, Holak T
15N NMR relaxation rates of mini-IGFBP-5, an N-terminal insulin-like growth factor binding domain of the insulin-like growth factor...
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[NMR paper] NMR study of the transforming growth factor-alpha (TGF-alpha)-epidermal growth factor
NMR study of the transforming growth factor-alpha (TGF-alpha)-epidermal growth factor receptor complex. Visualization of human TGF-alpha binding determinants through nuclear Overhauser enhancement analysis.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles NMR study of the transforming growth factor-alpha (TGF-alpha)-epidermal growth factor receptor complex. Visualization of human TGF-alpha binding determinants through nuclear Overhauser enhancement analysis.
J Biol...
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[NMR paper] 1H-NMR assignment and secondary structure of human insulin-like growth factor-I (IGF-
1H-NMR assignment and secondary structure of human insulin-like growth factor-I (IGF-I) in solution.
Related Articles 1H-NMR assignment and secondary structure of human insulin-like growth factor-I (IGF-I) in solution.
J Biochem. 1992 Apr;111(4):529-36
Authors: Sato A, Nishimura S, Ohkubo T, Kyogoku Y, Koyama S, Kobayashi M, Yasuda T, Kobayashi Y
Human insulin-like growth factor-I (IGF-I) was studied by two-dimensional 1H-NMR spectroscopy. Resonance assignments were obtained for all the backbone protons and almost all of the sidechain protons...
The insulin-like growth factor (IGF)binding protein 1 binding epitope on IGF-I probed
Linear Mode
