1n26

From Proteopedia

(Difference between revisions)

Current revision

Crystal Structure of the extra-cellular domains of Human Interleukin-6 Receptor alpha chain

Structural highlights

1n26 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.4Å
Ligands:	, , , , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 PubMed

Dysregulated production of IL-6 and its receptor (IL-6R) are implicated in the pathogenesis of multiple myeloma, autoimmune diseases and prostate cancer. The IL-6R complex comprises two molecules each of IL-6, IL-6R, and the signaling molecule, gp130. Here, we report the x-ray structure (2.4 A) of the IL-6R ectodomains. The N-terminal strand of the Ig-like domain (D(1)) is disulfide-bonded to domain D(2), and domains D(2) and D(3), the cytokine-binding domain, are structurally similar to known cytokine-binding domains. The head-to-tail packing of two closely associated IL-6R molecules observed in the crystal may be representative of the configuration of the physiological dimer of IL-6R and provides new insight into the architecture of the IL-6R complex.

Structure of the extracellular domains of the human interleukin-6 receptor alpha -chain.,Varghese JN, Moritz RL, Lou MZ, Van Donkelaar A, Ji H, Ivancic N, Branson KM, Hall NE, Simpson RJ Proc Natl Acad Sci U S A. 2002 Dec 10;99(25):15959-64. Epub 2002 Dec 2. PMID:12461182^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Martens AS, Bode JG, Heinrich PC, Graeve L. The cytoplasmic domain of the interleukin-6 receptor gp80 mediates its basolateral sorting in polarized madin-darby canine kidney cells. J Cell Sci. 2000 Oct;113 ( Pt 20):3593-602. PMID:11017875
↑ Buk DM, Renner O, Graeve L. Increased association with detergent-resistant membranes/lipid rafts of apically targeted mutants of the interleukin-6 receptor gp80. Eur J Cell Biol. 2005 Oct;84(10):819-31. PMID:16270750
↑ Martens AS, Bode JG, Heinrich PC, Graeve L. The cytoplasmic domain of the interleukin-6 receptor gp80 mediates its basolateral sorting in polarized madin-darby canine kidney cells. J Cell Sci. 2000 Oct;113 ( Pt 20):3593-602. PMID:11017875
↑ Buk DM, Renner O, Graeve L. Increased association with detergent-resistant membranes/lipid rafts of apically targeted mutants of the interleukin-6 receptor gp80. Eur J Cell Biol. 2005 Oct;84(10):819-31. PMID:16270750
↑ Varghese JN, Moritz RL, Lou MZ, Van Donkelaar A, Ji H, Ivancic N, Branson KM, Hall NE, Simpson RJ. Structure of the extracellular domains of the human interleukin-6 receptor alpha -chain. Proc Natl Acad Sci U S A. 2002 Dec 10;99(25):15959-64. Epub 2002 Dec 2. PMID:12461182 doi:http://dx.doi.org/10.1073/pnas.232432399

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1n26"

@@ Line 1: / Line 1: @@
 ==Crystal Structure of the extra-cellular domains of Human Interleukin-6 Receptor alpha chain==
-<StructureSection load='1n26' size='340' side='right' caption='[[1n26]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+<StructureSection load='1n26' size='340' side='right'caption='[[1n26]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1n26]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N26 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1N26 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1n26]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N26 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N26 FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CYS:CYSTEINE'>CYS</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene><br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4&#8491;</td></tr>
-<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1il6|1il6]], [[1i1r|1i1r]], [[1n2q|1n2q]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CYS:CYSTEINE'>CYS</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IL6R ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=1n26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n26 OCA], [https://pdbe.org/1n26 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n26 RCSB], [https://www.ebi.ac.uk/pdbsum/1n26 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n26 ProSAT]</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=1n26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n26 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1n26 RCSB], [http://www.ebi.ac.uk/pdbsum/1n26 PDBsum]</span></td></tr>
+</table>
-<table>
+== 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 ==
 [[Image:Consurf_key_small.gif|200px|right]]
 Check<jmol>
   <jmolCheckbox>
-    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n2/1n26_consurf.spt"</scriptWhenChecked>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n2/1n26_consurf.spt"</scriptWhenChecked>
-    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
-</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1n26 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">
@@ Line 26: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1n26" style="background-color:#fffaf0;"></div>
 ==See Also==
-*[[Interleukin receptor|Interleukin receptor]]
+*[[Interleukin receptor 3D structures|Interleukin receptor 3D structures]]
 == References ==
 <references/>
@@ Line 34: / Line 37: @@
 </StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Branson, K M.]]
+[[Category: Large Structures]]
-[[Category: Donkelaar, A van.]]
+[[Category: Branson KM]]
-[[Category: Hall, N E.]]
+[[Category: Hall NE]]
-[[Category: Ivancic, N.]]
+[[Category: Ivancic N]]
-[[Category: Ji, H.]]
+[[Category: Ji H]]
-[[Category: Lou, M Z.]]
+[[Category: Lou M-Z]]
-[[Category: Moritz, R L.]]
+[[Category: Moritz RL]]
-[[Category: Simpson, R J.]]
+[[Category: Simpson RJ]]
-[[Category: Varghese, J N.]]
+[[Category: Varghese JN]]
-[[Category: Cytokine]]
+[[Category: Van Donkelaar A]]
-[[Category: Glycoprotein]]
-[[Category: Immunoglobulin domain]]
-[[Category: Transmembrane]]

1n26

From Proteopedia

Current revision

Crystal Structure of the extra-cellular domains of Human Interleukin-6 Receptor alpha chain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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