Structure of the OsSERK2 leucine-rich repeat extracellular domain

SERK proteins play a central role in immune and developmental signaling pathways in plants. Structural studies have been performed in order to better understand the role of the OsSERK2 coreceptor in signaling with its partner receptors. Here, crystal structures of the LRR domains of OsSERK2 and a D128N OsSERK2 mutant, expressed as hagfish variable lymphocyte receptor (VLR) fusions, are reported.