Biochemical mapping of a ligand‐binding domain within Arabidopsis BAM1 reveals diversified ligand recognition mechanisms of plant LRR‐RKs

• Published in: The Plant journal : for cell and molecular biology Vol. 70; no. 5; pp. 845 - 854
• Main Authors: Shinohara, Hidefumi, Moriyama, Yuji, Ohyama, Kentaro, Matsubayashi, Yoshikatsu
• Format: Journal Article
• Language: English
• Published: Oxford, UK Blackwell Publishing Ltd 01.06.2012; Blackwell
• Subjects: Amino Acid Sequence; Arabidopsis; Arabidopsis - genetics; Arabidopsis - metabolism; Arabidopsis Proteins - genetics; Arabidopsis Proteins - metabolism; Binding Sites; Biochemistry; Biological and medical sciences; Cell receptors; Cell structures and functions; CLAVATA; Consensus Sequence; Electrophoresis, Polyacrylamide Gel; Enzymes; Fundamental and applied biological sciences. Psychology; Kinases; Leucine - metabolism; leucine‐rich repeat; ligand binding; Ligands; Miscellaneous; missense mutation; Molecular and cellular biology; Molecular Sequence Data; Mutagenesis, Site-Directed; mutants; Mutation; Mutation, Missense; Nicotiana - genetics; Nicotiana - metabolism; Peptide Fragments - metabolism; photoaffinity labeling; Photoaffinity Labels - metabolism; Plant biology; Plant physiology and development; Protein Binding; Protein Interaction Mapping - methods; Protein Serine-Threonine Kinases - genetics; Protein Serine-Threonine Kinases - metabolism; Protein Structure, Tertiary; receptor kinase; Receptor Protein-Tyrosine Kinases - genetics; Receptor Protein-Tyrosine Kinases - metabolism; secreted peptide; Sequence Alignment; Sequence Homology, Amino Acid; Ligand binding; Vegetals; Peptides; Enzyme; Ligand; Arabidopsis; Transferases; Leucine-rich repeat; Mechanism; Arabidopsis thaliana; Plant; Cruciferae; Kinase; Dicotyledones; Angiospermae; Spermatophyta; secreted peptide; CLAVATA; Recognition; Biological receptor; receptor kinase

Leucine‐rich repeat receptor kinases (LRR‐RKs) are the largest sub‐family of transmembrane receptor kinases in plants. In several LRR‐RKs, a loop‐out region called an ‘island domain’, which intercepts the extracellular tandem LRRs at a position near the transmembrane domain, constitutes the ligand‐b...