4gaf

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<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=4gaf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gaf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gaf RCSB], [http://www.ebi.ac.uk/pdbsum/4gaf PDBsum]</span></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=4gaf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gaf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gaf RCSB], [http://www.ebi.ac.uk/pdbsum/4gaf PDBsum]</span></td></tr>
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== Function ==
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[[http://www.uniprot.org/uniprot/IL1R1_HUMAN IL1R1_HUMAN]] Receptor for IL1A, IL1B and IL1RN. After binding to interleukin-1 associates with the corecptor IL1RAP to form the high affinity interleukin-1 receptor complex which mediates interleukin-1-dependent activation of NF-kappa-B, MAPK and other pathways. Signaling involves the recruitment of adapter molecules such as TOLLIP, MYD88, and IRAK1 or IRAK2 via the respective TIR domains of the receptor/coreceptor subunits. Binds ligands with comparable affinity and binding of antagonist IL1RN prevents association with IL1RAP to form a signaling complex.<ref>PMID:10671496</ref>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==

Revision as of 10:00, 25 December 2014

Crystal structure of EBI-005, a chimera of human IL-1beta and IL-1Ra, bound to human Interleukin-1 receptor type 1

4gaf, resolution 2.15Å

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