b'@article{Albrecht2006c,'b'\nTITLE = {Resistance proteins: molecular switches of plant defence},\nAUTHOR = {Takken, Frank L. and Albrecht, Mario and Tameling, Wladimir I.},\nLANGUAGE = {eng},\nLOCALID = {Local-ID: C125673F004B2D7B-8EB4E2D106B8DB00C125713A0066CB86-Albrecht2006c},\nYEAR = {2006},\nDATE = {2006},\nABSTRACT = {Specificity of the plant innate immune system is often conferred by resistance (R) proteins. Most R proteins contain leucine-rich repeats (LRRs), a central nucleotide-binding site (NBS) and a variable amino-terminal domain. The LRRs are mainly involved in recognition, whereas the amino-terminal domain determines signalling specificity. The NBS forms part of a nucleotide binding (NB)-ARC domain that presumably functions as a molecular switch. The conserved nature of NB-ARC proteins makes it possible to map mutations of R protein residues onto the crystal structures of related NB-ARC proteins, providing hypotheses for the functional roles of these residues. A functional model emerges in which the LRRs control the molecular state of the NB-ARC domain. Pathogen recognition triggers nucleotide-dependent conformational changes that might induce oligomerisation, thereby providing a scaffold for activation of downstream signalling components.},\nJOURNAL = {Current Opinion in Plant Biology},\nVOLUME = {9},\nPAGES = {383--390},\n}\n'