Barwin domain explained

Symbol:	Barwin
Barwin
Pfam:	PF00967
Pfam Clan:	CL0199
Interpro:	IPR001153
Prosite:	PDOC00619
Scop:	1bw3

In molecular biology, the barwin domain is a protein domain found in barwin ("barley wound-induced"), a basic protein isolated from aqueous extracts of barley seeds. Barwin is 125 amino acids in length, and contains six cysteine residues that combine to form three disulphide bridges. In the pathogenesis-related protein nomenclature, it is PR-4.^{[1] [2]} This domain is found in a 122 amino acid stretch in the C-terminal of the products of two wound-induced genes (win1 and win2;,) from potato, the product of the Pro-hevein gene of rubber trees, and pathogenesis-related protein 4 from tobacco . The high levels of similarity among these proteins, and their ability to bind saccharides, suggest that the barwin domain may be involved in a common defence mechanism in plants.

Notes and References

1. Svensson B, Svendsen I, Hojrup P, Roepstorff P, Ludvigsen S, Poulsen FM . Primary structure of barwin: a barley seed protein closely related to the C-terminal domain of proteins encoded by wound-induced plant genes . Biochemistry . 31 . 37 . 8767–70 . September 1992 . 1390663 . 10.1021/bi00152a012 .
2. Ludvigsen S, Poulsen FM . Secondary structure in solution of barwin from barley seed using 1H nuclear magnetic resonance spectroscopy . Biochemistry . 31 . 37 . 8771–82 . September 1992 . 1390664 . 10.1021/bi00152a013 .