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Insulin-like growth factor II receptor as a multifunctional binding protein
Nature
|September 24, 1987
Summary
The human insulin-like growth factor II receptor (IGF-II receptor) is a transmembrane protein. Its structure is similar to the cation-independent mannose-6-phosphate receptor, suggesting shared functions.
Area of Science:
- Molecular Biology
- Cell Biology
- Biochemistry
Background:
- The insulin-like growth factor II receptor (IGF-II receptor) plays a crucial role in cellular processes.
- Understanding the structural basis of IGF-II receptor function is essential for deciphering its biological roles.
Purpose of the Study:
- To elucidate the primary structure of the human IGF-II receptor.
- To identify structural similarities and potential functional relationships with other known receptors.
Main Methods:
- Prediction of the primary structure from complementary DNA (cDNA) sequence analysis.
- Bioinformatic analysis to identify functional domains and homologies.
Main Results:
- The human IGF-II receptor is a transmembrane molecule.
- It possesses a large extracellular domain with fifteen repeat sequences.
- A distinct region shows homology to the fibronectin collagen-binding domain.
Conclusions:
- The predicted structure of the IGF-II receptor reveals key functional domains.
- Structural and biochemical similarities suggest the IGF-II receptor is identical to the cation-independent mannose-6-phosphate receptor.