作者: Wei Hao , Sarah M. Collier , Peter Moffett , Jijie Chai
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摘要: The potato (Solanum tuberosum) disease resistance protein Rx has a modular arrangement that contains coiled-coil (CC), nucleotide-binding (NB), and leucine-rich repeat (LRR) domains mediates to virus X. N-terminal CC domain undergoes an intramolecular interaction with the NB-LRR region intermolecular cofactor RanGAP2 (Ran GTPase-activating 2). Here, we report crystal structure of in complex Trp-Pro-Pro (WPP) RanGAP2. reveals forms heterodimer RanGAP2, striking contrast homodimeric barley MLA10. Structure-based mutagenesis identified residues from both WPP are crucial for their function vitro vivo. Our results reveal molecular mechanism underlying identify distinct surfaces involved interactions.