Our deepest condolences go out to his family and friends, and to all those who had the privilege of working with him. Rest in peace, Amos. Your work will live on long after you are gone.
PROSITE documentation PDOC00244Plant thionins signature
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PURL: https://purl.expasy.org/prosite/documentation/PDOC00244
Thionins are small, basic, plant proteins generally toxic to animal cells [1]. They seem to exert their toxic effect at the level of the cell membrane but their exact function is not known. They consist of a polypeptide chain of forty five to fifty amino acids with three to four internal disulfide bonds. They are found in seeds but also in the cell wall of leaves [2]. Thionins are processed from larger precursor proteins [3]. Crambin [4], a hydrophobic plant seed protein, also belongs to this family. The pattern we developed to detect this family of proteins includes three of the six cysteine residues involved in disulfide bonds.
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xxCCxxxxxxxxxxxCxxxxxxxxxCxxxCxxCxxxxxCxxxxxxxx
************** |
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'C': conserved cysteine involved in a disulfide bond. '*': position of the pattern.Note:
The proteins from the γ-thionin family are not related to the above proteins and are described in a separate section.
Last update:May 2004 / Text revised.
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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Vernon L.P. Evett G.E. Zeikus R.D. Gray W.R. |
| Title | A toxic thionin from Pyrularia pubera: purification, properties, and amino acid sequence. | |
| Source | Arch. Biochem. Biophys. 238:18-29(1985). | |
| PubMed ID | 3985614 |
| 2 | Authors | Bohlmann H. Clausen S. Behnke S. Giese H. Hiller C. Reimann-Phillip U. Schrader G. Barkholt V. Apel K. |
| Source | EMBO J. 7:1559-1565(1988). |
| 3 | Authors | Bohlmann H. Apel K. |
| Source | Mol. Gen. Genet. 207:446-454(1987). |
| 4 | Authors | Teeter M.M. Mazer J.A. L'Italien J.J. |
| Title | Primary structure of the hydrophobic plant protein crambin. | |
| Source | Biochemistry 20:5437-5443(1981). | |
| PubMed ID | 6895315 |
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