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Plasma cell membrane glycoprotein PC-1. Primary structure deduced from cDNA clones
The Journal of Biological Chemistry
|April 5, 1987
Summary
The PC-1 protein, a membrane glycoprotein on antibody-secreting cells, has its mRNA and protein sequence detailed. Its unique transmembrane orientation and structure are revealed, resembling other key cell surface receptors.
Area of Science:
- Cell Biology
- Molecular Biology
- Immunology
Background:
- PC-1 protein is a membrane glycoprotein found on antibody-secreting cells.
- It comprises two disulfide-bonded polypeptides, each around 120,000 molecular weight.
Purpose of the Study:
- To elucidate the complete sequence of PC-1 mRNA and protein.
- To characterize the transmembrane orientation and structural features of the PC-1 protein.
Main Methods:
- mRNA sequencing
- Protein sequence analysis
- Bioinformatic analysis of protein structure and membrane topology.
Main Results:
- The PC-1 protein consists of 905 amino acids.
- It exhibits an unusual transmembrane orientation with 58 intracellular and 826 extracellular residues.
- A cysteine-rich region, potentially from exon duplication, is located near the extracellular surface.
Conclusions:
- The PC-1 protein possesses a distinct structure and membrane orientation.
- Its topology is similar to other important membrane glycoproteins like the transferrin receptor and Ia invariant chain.