Primary amino acid sequence of alpha-trichosanthin and molecular models for abrin A-chain and alpha-trichosanthin
Ricin A-chain, abrin A-chain, and alpha-trichosanthin are members of a larger group of proteins called ribosome-inactivating proteins. These proteins all function to catalytically inactivate eukaryotic 60 S ribosomal subunits leading to rapid shutdown of protein synthesis. They are homologous in seq...
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Veröffentlicht in: | The Journal of biological chemistry 1990-05, Vol.265 (15), p.8665-8669 |
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Sprache: | eng |
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Zusammenfassung: | Ricin A-chain, abrin A-chain, and alpha-trichosanthin are members of a larger group of proteins called ribosome-inactivating
proteins. These proteins all function to catalytically inactivate eukaryotic 60 S ribosomal subunits leading to rapid shutdown
of protein synthesis. They are homologous in sequence and are probably evolutionarily related. We have determined the complete
primary amino acid sequence of alpha-trichosanthin and have found it to be homologous, as expected, to that of abrin A-chain
and ricin A-chain. A crystal structure for ricin, which includes ricin A-chain and ricin B-chain, has been determined from
x-ray diffraction data. Based on the sequence homologies of these proteins, we fit the primary sequences of abrin A-chain
and alpha-trichosanthin to the backbone structure for ricin A-chain and have generated energy-minimized molecular models for
them. These models should prove useful in studying the structural-functional relationships of these proteins in particular
and of the class in general. |
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ISSN: | 0021-9258 1083-351X |
DOI: | 10.1016/S0021-9258(19)38939-2 |