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Specific recognition of two MAX effectors by integrated HMA domains in plant immune receptors involves distinct binding surfaces
Proceedings of the National Academy of Sciences of the United States of America
The structurally conserved but sequence-unrelated MAX (Magnaporthe oryzaeavirulence and ToxB-like) effectors AVR1-CO39 and AVR-PikD from the blast fungusM. oryzaeare recognized by the rice nucleotide-binding domain and leucine-rich repeat proteins (NLRs) RGA5 and Pikp-1, respectively. This involves, in both cases, direct interaction of the effector with a heavy metal-associated (HMA) integrated domain (ID) in the NLR. Here, we solved the crystal structures of a C-terminal fragment of RGA5doi:10.1073/pnas.1810705115 fatcat:qwu33bhmcjh7bdiz7rl7ukejlu