3jrn

<StructureSection load='3jrn' size='340' side='right' caption='[[3jrn]], [[Resolution|resolution]] 2.00&Aring;' scene=''>

<table><tr><td colspan='2'>[[3jrn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3JRN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3JRN FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ARS:ARSENIC'>ARS</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AT1G72930, At1g72930/F3N23.13, AtTIR, F3N23.13 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=3jrn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3jrn OCA], [http://pdbe.org/3jrn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3jrn RCSB], [http://www.ebi.ac.uk/pdbsum/3jrn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3jrn ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/TIR_ARATH TIR_ARATH]] Disease resistance protein. Resistance proteins guard the plant against pathogens that contain an appropriate avirulence protein via a direct or indirect interaction with this avirulence protein. That triggers a defense system including the hypersensitive response, which restricts the pathogen growth (By similarity).

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

Plants use a highly evolved immune system to exhibit defense response against microbial infections. The plant TIR domain, together with the nucleotide-binding (NB) domain and/or a LRR region, forms a type of molecule, named resistance (R) proteins, that interact with microbial effector proteins and elicit hypersensitive responses against infection. Here, we report the first crystal structure of a plant TIR domain from Arabidopsis thaliana (AtTIR) solved at a resolution of 2.0 A. The structure consists of five beta-strands forming a parallel beta-sheet at the core of the protein. The beta-strands are connected by a series of alpha-helices and the overall fold mimics closely that of other mammalian and bacterial TIR domains. However, the region of the alphaD-helix reveals significant differences when compared with other TIR structures, especially the alphaD3-helix that corresponds to an insertion only present in plant TIR domains. Available mutagenesis data suggest that several conserved and exposed residues in this region are involved in the plant TIR signaling function.

The crystal structure of a TIR domain from Arabidopsis thaliana reveals a conserved helical region unique to plants.,Chan SL, Mukasa T, Santelli E, Low LY, Pascual J Protein Sci. 2010 Jan;19(1):155-61. PMID:19845004<ref>PMID:19845004</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 3jrn" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Arath]]

[[Category: Chan, S L]]

[[Category: Low, L Y]]

[[Category: Mukasa, T]]

[[Category: Pascual, J]]

[[Category: Santelli, E]]

[[Category: Tir domain arabidopsis thaliana]]