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5jhj
From Proteopedia
(Difference between revisions)
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5jhj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jhj OCA], [http://pdbe.org/5jhj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jhj RCSB], [http://www.ebi.ac.uk/pdbsum/5jhj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jhj ProSAT]</span></td></tr> | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5jhj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jhj OCA], [http://pdbe.org/5jhj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jhj RCSB], [http://www.ebi.ac.uk/pdbsum/5jhj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jhj ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Nucleotide binding domain and leucine-rich repeat proteins (NLRs) are important receptors in plant immunity that allow recognition of pathogen effectors. The rice (Oryza sativa) NLR RGA5 recognizes the Magnaporthe oryzae effector AVR-Pia through direct interaction. Here, we gained detailed insights into the molecular and structural bases of AVR-Pia-RGA5 interaction and the role of the RATX1 decoy domain of RGA5. NMR titration combined with in vitro and in vivo protein-protein interaction analyses identified the AVR-Pia interaction surface that binds to the RATX1 domain. Structure-informed AVR-Pia mutants showed that, although AVR-Pia associates with additional sites in RGA5, binding to the RATX1 domain is necessary for pathogen recognition but can be of moderate affinity. Therefore, RGA5-mediated resistance is highly resilient to mutations in the effector. We propose a model that explains such robust effector recognition as a consequence, and an advantage, of the combination of integrated decoy domains with additional independent effector-NLR interactions. | ||
| + | |||
| + | Recognition of the Magnaporthe oryzae Effector AVR-Pia by the Decoy Domain of the Rice NLR Immune Receptor RGA5.,Ortiz D, de Guillen K, Cesari S, Chalvon V, Gracy J, Padilla A, Kroj T Plant Cell. 2017 Jan;29(1):156-168. doi: 10.1105/tpc.16.00435. Epub 2017 Jan 13. PMID:28087830<ref>PMID:28087830</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5jhj" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 07:02, 5 April 2017
M. Oryzae effector AVR-Pia mutant H3
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