4qdh

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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4qdh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qdh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qdh RCSB], [http://www.ebi.ac.uk/pdbsum/4qdh PDBsum]</span></td></tr>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4qdh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4qdh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4qdh RCSB], [http://www.ebi.ac.uk/pdbsum/4qdh PDBsum]</span></td></tr>
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== Publication Abstract from PubMed ==
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Toll-like receptors (TLRs) are important pattern recognition receptors that function in innate immunity. Elucidating the structure and signaling mechanisms of TLR9, a sensor of foreign and endogenous DNA, is essential for understanding its key role in immunity against microbial pathogens as well as in autoimmunity. Abundant evidence suggests that the TLR9-CTD (C-terminal domain) by itself is capable of DNA binding and signaling. The crystal structure of unliganded mouse TLR9-CTD is presented. TLR9-CTD exhibits one unique feature, a cluster of stacked aromatic and arginine side chains on its concave face. Overall, its structure is most related to the TLR8-CTD, suggesting a similar mode of ligand binding and signaling. Proteins 2014;. (c) 2014 Wiley Periodicals, Inc.
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Crystal structure of the C-terminal domain of mouse TLR9.,Collins B, Wilson IA Proteins. 2014 May 30. doi: 10.1002/prot.24616. PMID:24888966<ref>PMID:24888966</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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== References ==
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<references/>
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</StructureSection>

Revision as of 06:16, 2 July 2014

Crystal Structure of the C-terminal Domain of Mouse TLR9

4qdh, resolution 2.40Å

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