The effect of amino acid substitutions at position 342 on the secretion of human α1-antitrypsin from Xenopus oocytes
| Autor: | Richard C. Foreman, Ying Wu |
|---|---|
| Jazyk: | angličtina |
| Předmět: |
Oocyte
Protein Conformation α1-Antitrypsin secretion Lysine DNA Mutational Analysis Biophysics Xenopus In Vitro Techniques Z mutation Biochemistry Cell Line Residue (chemistry) Mice Structure-Activity Relationship Xenopus laevis Protein structure Structural Biology Genetics Animals Humans Amino Acid Sequence Site-directed mutagenesis Molecular Biology Peptide sequence chemistry.chemical_classification biology Cell Biology Glutamic acid biology.organism_classification Recombinant Proteins Amino acid chemistry alpha 1-Antitrypsin Oocytes Salts |
| Zdroj: | FEBS Letters. (1):21-23 |
| ISSN: | 0014-5793 |
| DOI: | 10.1016/0014-5793(90)80962-I |
| Popis: | A glutamic acid to lysine change in the Z variant of human alpha 1-antitrypsin is associated with a failure to secrete the protein from synthesising cells. The block in export of the protein may be caused either by the loss of an acidic residue or the introduction of a basic one at this point in the polypeptide chain. Site-directed mutagenesis has been used to construct novel alpha 1-antitrypsin mutants which show that the side chain interactions from Glu-342 are not obligatory for protein export and it is rather the introduction of a basic residue at this point which produces the intracellular accumulation of the protein. |
| Databáze: | OpenAIRE |
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