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The domain structure of the inhibitor subunit of human inter‐α‐trypsin inhibitor reflects the exon structure of its gene
Author(s) -
Vetr Helga,
Kögler Manuela,
Gebhard Wolfgang
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)80207-8
Subject(s) - trypsin inhibitor , exon , proteinase inhibitor , kunitz sti protease inhibitor , gene , coding region , peptide sequence , protein subunit , microbiology and biotechnology , protease inhibitor (pharmacology) , amino acid , biology , trypsin , chemistry , biochemistry , genetics , enzyme , virus , antiretroviral therapy , viral load
The gene coding for the inhibitor subunit of the human plasma protein complex inter‐α‐trypsin inhibitor has been cloned. The exon structure of the gene corresponds with the organization of the protein in two distinct inhibitor domains. The exons coding for the inhibitor domains each comprise the complete information for a typical Kunitz‐type proteinase inhibitor structure. In contrast to bovine aprotinin, the mature inhibitor protein contains amino acid residues flanking the inhibitor domains on both sides. These amino acid residues are encoded by additional exons.