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1il8

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(New page: 200px<br /> <applet load="1il8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1il8" /> '''THREE-DIMENSIONAL STRUCTURE OF INTERLEUKIN ...)
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[[Image:1il8.gif|left|200px]]<br />
 
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<applet load="1il8" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1il8" />
 
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'''THREE-DIMENSIONAL STRUCTURE OF INTERLEUKIN 8 IN SOLUTION'''<br />
 
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==Overview==
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==THREE-DIMENSIONAL STRUCTURE OF INTERLEUKIN 8 IN SOLUTION==
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The solution structure of the interleukin 8 (IL-8) dimer has been solved, by nuclear magnetic resonance (NMR) spectroscopy and hybrid distance, geometry-dynamical simulated annealing calculations. The structure, determination is based on a total of 1880 experimental distance restraints, (of which 82 are intersubunit) and 362 torsion angle restraints, (comprising phi, psi, and chi 1 torsion angles). A total of 30 simulated, annealing structures were calculated, and the atomic rms distribution, about the mean coordinate positions (excluding residues 1-5 of each, subunit) is 0.41 +/- 0.08 A for the backbone atoms and 0.90 +/- 0.08 A for, all atoms. The three-dimensional solution structure of the IL-8 dimer, reveals a structural motif in which two symmetry-related antiparallel, alpha-helices, approximately 24 A long and separated by about 14 A, lie on, top of a six-stranded antiparallel beta-sheet platform derived from two, three-stranded Greek keys, one from each monomer unit. The general, architecture is similar to that of the alpha 1/alpha 2 domains of the, human class I histocompatibility antigen HLA-A2. It is suggested that the, two alpha-helices form the binding site for the cellular receptor and that, the specificity of IL-8, as well as that of a number of related proteins, involved in cell-specific chemotaxis, mediation of cell growth, and the, inflammatory response, is achieved by the distinct distribution of charged, and polar residues at the surface of the helices.
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<StructureSection load='1il8' size='340' side='right'caption='[[1il8]]' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1il8]] is a 2 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=1IL8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IL8 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1il8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1il8 OCA], [https://pdbe.org/1il8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1il8 RCSB], [https://www.ebi.ac.uk/pdbsum/1il8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1il8 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/IL8_HUMAN IL8_HUMAN] IL-8 is a chemotactic factor that attracts neutrophils, basophils, and T-cells, but not monocytes. It is also involved in neutrophil activation. It is released from several cell types in response to an inflammatory stimulus. IL-8(6-77) has a 5-10-fold higher activity on neutrophil activation, IL-8(5-77) has increased activity on neutrophil activation and IL-8(7-77) has a higher affinity to receptors CXCR1 and CXCR2 as compared to IL-8(1-77), respectively.<ref>PMID:2145175</ref> <ref>PMID:2212672</ref> <ref>PMID:11978786</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/il/1il8_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1il8 ConSurf].
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<div style="clear:both"></div>
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==Disease==
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==See Also==
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Known disease associated with this structure: AIDS, slow progression to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=146929 146929]]
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*[[Interleukin 3D structures|Interleukin 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1IL8 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=1IL8 OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Three-dimensional structure of interleukin 8 in solution., Clore GM, Appella E, Yamada M, Matsushima K, Gronenborn AM, Biochemistry. 1990 Feb 20;29(7):1689-96. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2184886 2184886]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Clore, G.M.]]
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[[Category: Clore GM]]
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[[Category: Gronenborn, A.M.]]
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[[Category: Gronenborn AM]]
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[[Category: cytokine]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:31:05 2007''
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Current revision

THREE-DIMENSIONAL STRUCTURE OF INTERLEUKIN 8 IN SOLUTION

PDB ID 1il8

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