How to build a pathogen detector: structural basis of NB-LRR function

F.L.W. Takken, A. Goverse

Research output: Contribution to journalArticleAcademicpeer-review

145 Citations (Scopus)


Many plant disease resistance (R) proteins belong to the family of nucleotide-binding-leucine rich repeat (NB-LRR) proteins. NB-LRRs mediate recognition of pathogen-derived effector molecules and subsequently activate host defence. Their multi-domain structure allows these pathogen detectors to simultaneously act as sensor, switch and response factor. Structure–function analyses and the recent elucidation of the 3D structures of subdomains have provided new insight in how these different functions are combined and what the contribution is of the individual subdomains. Besides interdomain contacts, interactions with chaperones, the proteasome and effector baits are required to keep NB-LRRs in a signalling-competent, yet auto-inhibited state. In this review we explore operational models of NB-LRR functioning based on recent advances in understanding their structure
Original languageEnglish
Pages (from-to)375-384
JournalCurrent Opinion in Plant Biology
Issue number4
Publication statusPublished - 2012


  • disease resistance protein
  • tobacco-mosaic-virus
  • rich repeat protein
  • c-terminal domain
  • cell-death
  • coiled-coil
  • flax rust
  • effector recognition
  • crystal-structure
  • arabidopsis eds1

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