1il6: Difference between revisions

New page: left|200px<br /> <applet load="1il6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1il6" /> '''HUMAN INTERLEUKIN-6, NMR, MINIMIZED AVERAGE...
 
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'''HUMAN INTERLEUKIN-6, NMR, MINIMIZED AVERAGE STRUCTURE'''<br />


==Overview==
==HUMAN INTERLEUKIN-6, NMR, MINIMIZED AVERAGE STRUCTURE==
Interleukin-6 (IL-6) is a 185 amino acid cytokine which exerts multiple, biological effects in vivo and whose dysregulation underlies several, disease processes. The solution structure of recombinant human, interleukin-6 has now been determined using heteronuclear three and, four-dimensional NMR spectroscopy. The structure of the molecule was, determined using 3044 distance and torsion restraints derived by NMR, spectroscopy to generate an ensemble of 32 structures using a combined, distance geometry/simulated annealing protocol. The protein contains five, alpha-helices interspersed with variable-length loops; four of these, helices constitute a classical four-helix bundle with the fifth helix, located in the CD loop. There were no distance violations greater than 0.3, A in any of the final 32 structures and the ensemble has an, average-to-the-mean backbone root-mean-square deviation of 0.50 A for the, core four-helix bundle. Although the amino-terminal 19 amino acids are, disordered in solution, the remainder of the molecule has a well defined, structure that shares many features displayed by other long-chain, four-helix bundle cytokines. The high-resolution NMR structure of hIL-6 is, used to rationalize available mutagenesis data in terms of a heteromeric, receptor complex.
<StructureSection load='1il6' size='340' side='right'caption='[[1il6]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1il6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IL6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IL6 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 1 model</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=1il6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1il6 OCA], [https://pdbe.org/1il6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1il6 RCSB], [https://www.ebi.ac.uk/pdbsum/1il6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1il6 ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/IL6_HUMAN IL6_HUMAN] Genetic variations in IL6 are associated with susceptibility to rheumatoid arthritis systemic juvenile (RASJ) [MIM:[https://omim.org/entry/604302 604302]. An inflammatory articular disorder with systemic-onset beginning before the age of 16. It represents a subgroup of juvenile arthritis associated with severe extraarticular features and occasionally fatal complications. During active phases of the disorder, patients display a typical daily spiking fever, an evanescent macular rash, lymphadenopathy, hepatosplenomegaly, serositis, myalgia and arthritis.  Note=A IL6 promoter polymorphism is associated with a lifetime risk of development of Kaposi sarcoma in HIV-infected men.
== Function ==
[https://www.uniprot.org/uniprot/IL6_HUMAN IL6_HUMAN] Cytokine with a wide variety of biological functions. It is a potent inducer of the acute phase response. Plays an essential role in the final differentiation of B-cells into Ig-secreting cells Involved in lymphocyte and monocyte differentiation. It induces myeloma and plasmacytoma growth and induces nerve cells differentiation Acts on B-cells, T-cells, hepatocytes, hematopoietic progenitor cells and cells of the CNS. Also acts as a myokine. It is discharged into the bloodstream after muscle contraction and acts to increase the breakdown of fats and to improve insulin resistance.
== 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/il/1il6_consurf.spt"</scriptWhenChecked>
    <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/main_output.php?pdb_ID=1il6 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Interleukin-6 (IL-6) is a 185 amino acid cytokine which exerts multiple biological effects in vivo and whose dysregulation underlies several disease processes. The solution structure of recombinant human interleukin-6 has now been determined using heteronuclear three and four-dimensional NMR spectroscopy. The structure of the molecule was determined using 3044 distance and torsion restraints derived by NMR spectroscopy to generate an ensemble of 32 structures using a combined distance geometry/simulated annealing protocol. The protein contains five alpha-helices interspersed with variable-length loops; four of these helices constitute a classical four-helix bundle with the fifth helix located in the CD loop. There were no distance violations greater than 0.3 A in any of the final 32 structures and the ensemble has an average-to-the-mean backbone root-mean-square deviation of 0.50 A for the core four-helix bundle. Although the amino-terminal 19 amino acids are disordered in solution, the remainder of the molecule has a well defined structure that shares many features displayed by other long-chain four-helix bundle cytokines. The high-resolution NMR structure of hIL-6 is used to rationalize available mutagenesis data in terms of a heteromeric receptor complex.


==Disease==
Solution structure of recombinant human interleukin-6.,Xu GY, Yu HA, Hong J, Stahl M, McDonagh T, Kay LE, Cumming DA J Mol Biol. 1997 May 2;268(2):468-81. PMID:9159484<ref>PMID:9159484</ref>
Known diseases associated with this structure: Kaposi sarcoma, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=147620 147620]], Osteopenia/osteoporosis OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=147620 147620]]


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1IL6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IL6 OCA].
</div>
<div class="pdbe-citations 1il6" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Solution structure of recombinant human interleukin-6., Xu GY, Yu HA, Hong J, Stahl M, McDonagh T, Kay LE, Cumming DA, J Mol Biol. 1997 May 2;268(2):468-81. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9159484 9159484]
*[[Interleukin 3D structures|Interleukin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Cumming, D.A.]]
[[Category: Cumming DA]]
[[Category: Hong, J.]]
[[Category: Hong J]]
[[Category: Kay, L.E.]]
[[Category: Kay LE]]
[[Category: Mcdonagh, T.]]
[[Category: Mcdonagh T]]
[[Category: Stahl, M.]]
[[Category: Stahl M]]
[[Category: Xu, G.Y.]]
[[Category: Xu GY]]
[[Category: Yu, H.A.]]
[[Category: Yu HA]]
[[Category: cytokine]]
[[Category: glycoprotein]]
[[Category: growth factor]]
 
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