학술논문

Structure of the OsSERK2 leucine‐rich repeat extracellular domain
Document Type
article
Source
Acta Crystallographica Section D, Structural Biology. 70(11)
Subject
Biochemistry and Cell Biology
Biological Sciences
Amino Acid Sequence
Animals
Cell Line
Crystallography
X-Ray
Leucine Zippers
Models
Molecular
Molecular Sequence Data
Oryza
Plant Proteins
Point Mutation
Protein Conformation
Protein Kinases
Protein Structure
Tertiary
Recombinant Fusion Proteins
OsSERK2
SERKs
leucine-rich repeats
Physical Sciences
Chemical Sciences
Biophysics
Biological sciences
Chemical sciences
Physical sciences
Language
Abstract
Somatic embryogenesis receptor kinases (SERKs) are leucine-rich repeat (LRR)-containing integral membrane receptors that are involved in the regulation of development and immune responses in plants. It has recently been shown that rice SERK2 (OsSERK2) is essential for XA21-mediated resistance to the pathogen Xanthomonas oryzae pv. oryzae. OsSERK2 is also required for the BRI1-mediated, FLS2-mediated and EFR-mediated responses to brassinosteroids, flagellin and elongation factor Tu (EF-Tu), respectively. Here, crystal structures of the LRR domains of OsSERK2 and a D128N OsSERK2 mutant, expressed as hagfish variable lymphocyte receptor (VLR) fusions, are reported. These structures suggest that the aspartate mutation does not generate any significant conformational change in the protein, but instead leads to an altered interaction with partner receptors.