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PROSITE documentation PDOC00619 [for PROSITE entry PS00772]

Barwin domain signatures and profile





Description

Barwin [1] is a barley seed protein of 125 residues that binds weakly a chitin analog. It contains six cysteines involved in disulfide bonds, as shown in the following schematic representation.

                              +---------------+
                              |    *****      |                ****
    xxxxxxxxxxxxxxxCxxxxxxxxxxCxxxxCxCxxxxxxxxCxxxxxxxxxxxxxxxxxxCx
                   |               | |                           |
                   +---------------+ +---------------------------+
'C': conserved cysteine involved in a disulfide bond.
'*': position of the patterns.

Barwin is closely related to the following proteins:

  • Hevein, a wound-induced protein found in the latex of rubber trees.
  • HEL, an Arabidopsis thaliana hevein-like protein [2].
  • Win1 and win2, two wound-induced proteins from potato.
  • Pathogenesis-related protein 4 from tobacco.

Hevein and the win1/2 proteins consist of an N-terminal chitin-binding domain followed by a barwin-like C-terminal domain of ~122 residues. Barwin and its related proteins could be involved in a defense mechanism in plants [1].

The dominating structural feature of the barwin domain is a well-defined four-stranded antiparallel β-sheet, two parallel β-sheets packed antiparallel to each other and four short α-helices (see <PDB:1BW3>) [3].

As signature patterns, we selected two highly conserved regions that contain some of the cysteines. We also developed a profile that covers the entire barwin domain.

Last update:

December 2005 / Text revised; profile added.

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Technical section

PROSITE methods (with tools and information) covered by this documentation:

BARWIN_2, PS00772; Barwin domain signature 2  (PATTERN)

BARWIN_3, PS51174; Barwin domain profile  (MATRIX)

BARWIN_1, PS00771; Barwin domain signature 1  (PATTERN)


References

1AuthorsSvensson B. Svendsen I. Hoejrup P. Roepstorff P. Ludvigsen S. Poulsen F.M.
TitlePrimary structure of barwin: a barley seed protein closely related to the C-terminal domain of proteins encoded by wound-induced plant genes.
SourceBiochemistry 31:8767-8770(1992).
PubMed ID1390663

2AuthorsPotter S. Uknes S. Lawton K. Winter A.M. Chandler D. Dimaio J. Novitzky R. Ward E. Ryals J.
TitleRegulation of a hevein-like gene in Arabidopsis.
SourceMol. Plant Microbe Interact. 6:680-685(1993).
PubMed ID8118053

3AuthorsLudvigsen S. Poulsen F.M.
TitleThree-dimensional structure in solution of barwin, a protein from barley seed.
SourceBiochemistry 31:8783-8789(1992).
PubMed ID1390665



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