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Lectin Receptor Kinases in Plants

Authors :
Bernard Lescure
Christine Hervé
Pierre Rougé
Annick Barre
Source :
Critical Reviews in Plant Sciences. 21:379-399
Publication Year :
2002
Publisher :
Informa UK Limited, 2002.

Abstract

Referee: Dr. Philip Becraft, Zoology and Genetics/Agronomy Depts., 2116 Molecular Building, lowa State University, Ames, IA 50011 Forty-two lectin receptor kinase (lecRK)-related sequences and nine related soluble legume lectin sequences were identified in the Arabidopsis thaliana genome. The genes are scattered as a single or gathered copies at different loci throughout the five chromosomes, and four predicted lecRK probably correspond to pseudogenes. Both structural alignments and molecular modeling revealed striking similarities between the lectinlike domain of lecRK, and related A. thaliana soluble lectins and legume lectins. The hydrophobic cavity is extremely conserved, whereas most of the residues forming the monosaccharide-binding site and the bivalent cation-binding site of legume lectins are poorly conserved. LecRK should be unable to bind the simple sugars usually recognized by genuine legume lectins. Molecular modeling of the kinase domain suggests that, except for two apparently inactive rece...

Details

ISSN :
15497836 and 07352689
Volume :
21
Database :
OpenAIRE
Journal :
Critical Reviews in Plant Sciences
Accession number :
edsair.doi...........22e4baf152c98dcd227e8006819e802a
Full Text :
https://doi.org/10.1080/0735-260291044287