7d9m

<table><tr><td colspan='2'>[[7d9m]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Cteid Cteid]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7D9M OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7D9M FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IL-2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7959 CTEID])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=7d9m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7d9m OCA], [http://pdbe.org/7d9m PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7d9m RCSB], [http://www.ebi.ac.uk/pdbsum/7d9m PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7d9m ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Interleukin (IL) -2, a member of the four alpha-helical cytokine family, has broad regulatory roles in mediating vertebrate immune response. In mammals, IL-2 and IL-15 share a common evolutionary origin and possess overlapping but distinct functions. IL-2 and IL-15 bind to distinct private receptors for signaling. However, fish appear to possess a single IL-15Ralpha like gene whilst lack additional gene(s) coding for IL-2Ralpha. Whether the IL-2 and IL-15 interact with the same receptor in fish and how their functions and receptors have evolved are not fully understood. In this study, homologues of IL-2 and IL-2/15Ralpha were sequenced from a teleost species, grass carp (Ctenopharyngodon idella), and the crystal structure of IL-2 was determined. The grass carp IL-2 (termed CiIL-2) displayed a classical cytokine structure consisting of four helical bundles which shares significant similarity with human IL-15. The key amino acids involved in the interface interaction of IL-2/15 and their receptors are well conserved. The CiIL-2 has been shown to bind the IL-2/15Ralpha like homologue with an affinity of 2.45 nM, supporting the notion that fish IL-2 and IL-15 may share a single common private receptor for exerting functions. Syntenic analysis suggests that the IL-2Ralpha of tetrapods has evolved from an IL-15Ralpha like homologue, in which a second sushi domain (D2) in the extracellular region has been duplicated to facilitate the specific interaction with IL-2. The CiIL-2 was predominantly expressed in lymphocyte-rich tissues such as the spleen, kidney and thymus, and could be induced by PHA and IL-21. In vivo challenge with grass carp reovirus and Flavobacterium columnare also resulted in upregulation of CiIL-2 expression. The recombinant CiIL-2 was shown to activate expression of STAT5b, IL-1beta, IL-22 and IFN-gamma, and to promote the proliferation of the primary cell cultures from head kidney leucocytes. Our results shed lights into the co-evolution of IL-2 and its private receptor, and the functional divergence of IL-2 and IL-15 during evolution.

 

== References ==

[[Category: Cteid]]

[[Category: Jun, z]]

[[Category: Junya, w]]

[[Category: Interleukin-2]]