1ga3: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ga3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GA3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GA3 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1ga3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GA3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1GA3 FirstGlance]. <br> | ||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IL13 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IL13, NC30 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=1ga3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ga3 OCA], [http://pdbe.org/1ga3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ga3 RCSB], [http://www.ebi.ac.uk/pdbsum/1ga3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ga3 ProSAT]</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=1ga3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ga3 OCA], [http://pdbe.org/1ga3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ga3 RCSB], [http://www.ebi.ac.uk/pdbsum/1ga3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ga3 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
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[[Category: Horita, D A]] | [[Category: Horita, D A]] | ||
[[Category: Cytokine]] | [[Category: Cytokine]] | ||
Revision as of 12:30, 26 February 2020
NMR STRUCTURE OF INTERLEUKIN-13NMR STRUCTURE OF INTERLEUKIN-13
Structural highlights
Disease[IL13_HUMAN] Defects in IL13 may be a cause of susceptibility to allergic rhinitis (ALRH) [MIM:607154]. Allergic rhinitis is a common disease of complex inheritance and is characterized by mucosal inflammation caused by allergen exposure. Function[IL13_HUMAN] Cytokine. Inhibits inflammatory cytokine production. Synergizes with IL2 in regulating interferon-gamma synthesis. May be critical in regulating inflammatory and immune responses. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe complex and interrelated function of the interleukin cytokines relies on a range of pro-inflammatory and anti-inflammatory immune responses mediated by an array of receptors, and there is considerable cross-reactivity for related cytokines. Recent findings continue to elucidate the expression patterns of interleukin receptors associated with a range of diseases, including cancer. We report here the first experimentally determined high-resolution structure of human interleukin-13 (IL-13). The experimental structure is significantly different from an earlier homology model, which could have led to improper estimation of receptor interaction surfaces and design of mutational experiments. Similarities between the presented IL-13 structure and the homologous interleukin-4 (IL-4) are discussed. Additionally, mutation data for IL-4 and IL-13 are analyzed and combined with a detailed structural analysis of the IL-4/IL4Ralpha interface that leads us to postulate interactions at the IL-13/receptor interface. The structural comparison is used to interpret the different affinities for various receptors and establishes the basis for further mutational experiments and antagonist design. Solution structure of interleukin-13 and insights into receptor engagement.,Eisenmesser EZ, Horita DA, Altieri AS, Byrd RA J Mol Biol. 2001 Jun 29;310(1):231-41. PMID:11419949[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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