Abstract
The primary structure of human insulin-like growth factor II receptor, predicted from the complementary DNA sequence, reveals a transmembrane receptor molecule with a large extracellular domain made up of fifteen repeat sequences and a small region homologous to the collagen-binding domain of fibronectin. The structural and biochemical features of the IGF-II receptor appear identical to those of the cation-independent mannose-6-phosphate receptor.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Base Sequence
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Carrier Proteins
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DNA / genetics
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DNA, Recombinant
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Humans
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Membrane Proteins
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Oocytes / metabolism
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Rats
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Receptor, IGF Type 2
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Receptor, Insulin* / biosynthesis
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Receptor, Insulin* / genetics
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Receptor, Insulin* / isolation & purification
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Receptors, Somatomedin
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Repetitive Sequences, Nucleic Acid
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Sequence Homology, Nucleic Acid
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Xenopus laevis
Substances
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Carrier Proteins
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DNA, Recombinant
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Membrane Proteins
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Receptor, IGF Type 2
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Receptors, Somatomedin
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DNA
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Receptor, Insulin