STRUCTURAL FEATURES OF PLANT CHITINASES AND CHITIN-BINDING PROTEINSBEINTEMA, JJ., 22-Aug-1994, In : FEBS Letters. 350, 2-3, p. 159-163 5 p.
Research output: Contribution to journal › Review article › Academic › peer-review
Structural features of plant chitinases and chitin-binding proteins are discussed. Many of these proteins consist of multiple domains,of which the chitin-binding hevein domain is a predominant one. X-ray and NMR structures of representatives of the major classes of these proteins are available now, and are used to describe the structures of the other ones. Conserved positions of Cys residues can be taken as evidence for identically located disulfide bridges or cysteine residues. The current classification of chitinases is unsatisfactory and needs to be replaced by an evolutionarily more correct one. As the currently known three-dimensional structures of chitinases are those from barley and the rubber tree, Hevea brasiliensis, it is proposed to adopt the designation b-type (classes I, II and IV) and h-type (classes III and V) chitinases, respectively.
|Number of pages||5|
|Publication status||Published - 22-Aug-1994|
- CHITINASE, CHITIN-BINDING PROTEIN, LECTIN, AGGLUTININ, DISULFIDE BRIDGE, PR PROTEIN, CYSTEINE-RICH DOMAIN, MESSENGER-RNA ACCUMULATION, URTICA-DIOICA AGGLUTININ, TREE HEVEA-BRASILIENSIS, WHEAT-GERM-AGGLUTININ, CLASS-I CHITINASE, CRYSTAL-STRUCTURE, BARLEY SEED, MOLECULAR CHARACTERIZATION, DIFFERENTIAL EXPRESSION