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

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dc.contributor.authorForbes, B.
dc.contributor.authorMcNeil, K.
dc.contributor.authorScott, C.
dc.contributor.authorSurinya, K.
dc.contributor.authorCosgrove, L.
dc.contributor.authorWallace, J.
dc.date.issued2001
dc.description.abstractThe 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.
dc.identifier.citationGrowth Factors, 2001; 19(3):163-173
dc.identifier.doi10.3109/08977190109001084
dc.identifier.issn0897-7194
dc.identifier.issn1029-2292
dc.identifier.urihttp://hdl.handle.net/2440/28113
dc.language.isoen
dc.publisherHarwood Acad Publ GMBH
dc.source.urihttps://doi.org/10.3109/08977190109001084
dc.subjectCell Membrane
dc.subjectPlacenta
dc.subjectAnimals
dc.subjectHumans
dc.subjectRats
dc.subjectCations
dc.subjectReceptor, IGF Type 1
dc.subjectPeptides
dc.subjectInsulin-Like Growth Factor II
dc.subjectProteins
dc.subjectReceptor, IGF Type 2
dc.subjectRecombinant Proteins
dc.subjectCross-Linking Reagents
dc.subjectLigands
dc.subjectProtein Structure, Tertiary
dc.subjectProtein Binding
dc.subjectProtein Folding
dc.subjectDose-Response Relationship, Drug
dc.subjectKinetics
dc.subjectMutation
dc.subjectPlasmids
dc.subjectModels, Molecular
dc.subjectTime Factors
dc.titleContribution of residues A54 and L55 of the human insulin-like growth factor-II (IGF-II) A domain to Type 2 IGF receptor binding specificity
dc.typeJournal article
pubs.publication-statusPublished

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