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.

doi:10.3109/08977190109001084

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Article

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.

Growth factors (Chur, Switzerland) - 1 Jan 2001

Forbe B E, McNeil K A, Scott C D, Surinya K H, Cosgrove L J, Wallace J C

Abstract excerpt

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...

Topics

Animals
Cations
Cell Membrane
Cross-Linking Reagents
Dose-Response Relationship, Drug
Humans
Insulin-Like Growth Factor II
Kinetics
Ligands
Models, Molecular
Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Peptides

Placenta

Plasmids

Protein Binding

Protein Folding

Protein Structure, Tertiary

Proteins

Source

Open in PubMed

Identifiers

PMID: 11811790
DOI: 10.3109/08977190109001084

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