Dissection and Manipulation of LRR Domains in Plant Disease Resistance Gene Products.
- Univ. of Wisconsin, Madison, WI (United States)
Leucine-rich repeat (LRR) protein domains offer a readily diversifiable platform - literally, an extended protein surface - for specific binding of very diverse ligands. The project addressed the following overlapping research questions: How do leucine-rich repeat proteins recognize their cognate ligands? What are the intra- and inter-molecular transitions that occur that cause transmembrane LRR proteins to switch between off and on states? How do plants use LRR receptor proteins to activate disease resistance? Can we synthetically evolve new LRR proteins that have acquired new ligand specificities?
- Research Organization:
- Univ. of Wisconsin, Madison, WI (United States)
- Sponsoring Organization:
- USDOE Office of Science (SC), Basic Energy Sciences (BES)
- DOE Contract Number:
- FG02-02ER15342
- OSTI ID:
- 1055768
- Report Number(s):
- DOE; MSN107807/144-LH31
- Country of Publication:
- United States
- Language:
- English
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