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https://hdl.handle.net/2440/28113
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Type: | Journal article |
Title: | Contribution of residues A54 and L55 of the human insulin-like growth factor-II (IGF-II) A domain to Type 2 IGF receptor binding specificity |
Author: | Forbes, B. McNeil, K. Scott, C. Surinya, K. Cosgrove, L. Wallace, J. |
Citation: | Growth Factors, 2001; 19(3):163-173 |
Publisher: | Harwood Acad Publ GMBH |
Issue Date: | 2001 |
ISSN: | 0897-7194 1029-2292 |
Abstract: | The underlying specificity of the interaction between insulin-like growth factor-II (IGF-II) and mammalian Type 2 insulin-like growth factor/cation-independent mannose 6 phosphate receptor (IGF2R) is not understood. We have mutated residues A54 and L55 of IGF-II in the second A domain helix to arginine (found in the corresponding positions of IGF-I) and measured IGF2R binding. There is a 4- and 3.3-fold difference in dissociation constants for A54R IGF-II and L55R IGF-II, respectively, and a 6.6-fold difference for A54R L55R IGF-II compared with IGF-II as measured by BlAcore analysis using purified rat IGF2R. This is also confirmed using cross-linking and soluble rat placental membrane receptor binding assays. Binding to the type I IGF receptor (IGF1R) and IGF binding protein-2 (IGFBP-2) is not altered. We can, therefore, conclude that residues at positions 54 and 55 in IGF-II are important for and equally contribute to IGF2R binding. |
Keywords: | Cell Membrane Placenta Animals Humans Rats Cations Receptor, IGF Type 1 Peptides Insulin-Like Growth Factor II Proteins Receptor, IGF Type 2 Recombinant Proteins Cross-Linking Reagents Ligands Protein Structure, Tertiary Protein Binding Protein Folding Dose-Response Relationship, Drug Kinetics Mutation Plasmids Models, Molecular Time Factors |
DOI: | 10.3109/08977190109001084 |
Published version: | http://dx.doi.org/10.3109/08977190109001084 |
Appears in Collections: | Aurora harvest 6 Molecular and Biomedical Science publications |
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