Barwin domain

From Wikipedia, the free encyclopedia
Jump to navigation Jump to search
PDB 1bw4 EBI.jpg
three-dimensional structure in solution of barwin, a protein from barley seed
Symbol Barwin
Pfam PF00967
Pfam clan CL0199
InterPro IPR001153
SCOP 1bw3

In molecular biology, the barwin domain is a protein domain found in barwin, 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.[1][2] Comparative analysis shows the sequence of barwin to be highly similar to 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 hevein gene of rubber trees, and pathogenesis-related protein 4 from tobacco. The high levels of similarity to these proteins, and their ability to bind saccharides, suggest that the barwin domain may be involved in a common defence mechanism in plants.


  1. ^ Svensson B, Svendsen I, Hojrup P, Roepstorff P, Ludvigsen S, Poulsen FM (September 1992). "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. doi:10.1021/bi00152a012. PMID 1390663. 
  2. ^ Ludvigsen S, Poulsen FM (September 1992). "Secondary structure in solution of barwin from barley seed using 1H nuclear magnetic resonance spectroscopy". Biochemistry. 31 (37): 8771–82. doi:10.1021/bi00152a013. PMID 1390664. 

This article incorporates text from the public domain Pfam and InterPro IPR001153