2arw: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
<StructureSection load='2arw' size='340' side='right'caption='[[2arw]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | <StructureSection load='2arw' size='340' side='right'caption='[[2arw]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2arw]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2arw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2ARW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2ARW FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2arw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2arw OCA], [https://pdbe.org/2arw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2arw RCSB], [https://www.ebi.ac.uk/pdbsum/2arw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2arw ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/IL6RA_HUMAN IL6RA_HUMAN]] Part of the receptor for interleukin 6. Binds to IL6 with low affinity, but does not transduce a signal. Signal activation necessitate an association with IL6ST. Activation may lead to the regulation of the immune response, acute-phase reactions and hematopoiesis.<ref>PMID:11017875</ref> <ref>PMID:16270750</ref> Low concentration of a soluble form of IL6 receptor acts as an agonist of IL6 activity.<ref>PMID:11017875</ref> <ref>PMID:16270750</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 09:45, 1 December 2021
The solution structure of the membrane proximal cytokine receptor domain of the human interleukin-6 receptorThe solution structure of the membrane proximal cytokine receptor domain of the human interleukin-6 receptor
Structural highlights
Function[IL6RA_HUMAN] Part of the receptor for interleukin 6. Binds to IL6 with low affinity, but does not transduce a signal. Signal activation necessitate an association with IL6ST. Activation may lead to the regulation of the immune response, acute-phase reactions and hematopoiesis.[1] [2] Low concentration of a soluble form of IL6 receptor acts as an agonist of IL6 activity.[3] [4] 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 members of the interleukin-6-type family of cytokines interact with receptors that have a modular structure and are built of several immunoglobulin-like and fibronectin type III-like domains. These receptors have a characteristic cytokine receptor homology region consisting of two fibronectin type III-like domains defined by a set of four conserved cysteines and a tryptophan-serine-X-tryptophan-serine sequence motif. On target cells, interleukin-6 (IL-6) initially binds to its cognate alpha-receptor and subsequently to a homodimer of the signal transducer receptor gp130. The IL-6 receptor (IL-6R) consists of three extracellular domains. The N-terminal immunoglobulin-like domain is not involved in ligand binding, whereas the third membrane-proximal fibronectin-like domain (IL-6R-D3) accounts for more than 90% of the binding energy to IL-6. Here, we present the solution structure of the IL-6R-D3 domain solved by multidimensional heteronuclear NMR spectroscopy. The solution structure of the membrane-proximal cytokine receptor domain of the human interleukin-6 receptor.,Hecht O, Dingley AJ, Schwanter A, Ozbek S, Rose-John S, Grotzinger J Biol Chem. 2006 Sep;387(9):1255-9. PMID:16972794[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||