Author/Editor		Križaj, I; Drobnič-Košorok, M; Brzin, J; Jerala, R; Turk, V
Title		The primary structure of inhibitor cysteine proteinase from potato
Type		članek
Source		FEBS Lett
Vol. and No.		Letnik 333, št. 1-2
Publication year		1993
Volume		str. 15-20
Language		eng
Abstract		The complete amino acid sequence of the cysteine proteinase inhibitor from potato tubers determined. The inhibitor is a single protein having 180 amino acid residues. Its primary structure was elucidated by automatic degradation of the intact protein and sequnce analysis of peptides generated by CNBr, trypsin and glycyl endopeptidase. A search through the protein sequnece database showed homology to other plant proteinase inhibitors of differnet specificities and non-inhibitory proteins of M, around 20.000. On the basis of the sequnce homology, prediction of secondary structure and fold compability, based on a 3D-1D score to the three dimensional profile of Erythrina caffra trypsin inhibitor, we suggest that the potato cysteine proteinase inhibitor belongs to the superfamily of proteins that have the same pattern of three dimensional structure as soybean trypsin inhibitor. This superfamily would therefore include proteins that inhibit three different classes of proteinase - serine, cysteine and aspartic proteinases.
Descriptors		CYSTEINE PROTEINASE INHIBITORS AMINO ACID SEQUENCE POTATOES TRYPSIN INHIBITOR, KUNITZ SOYBEAN