1ikl

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[[Image:1ikl.jpg|left|200px]]
 
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{{Structure
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==NMR study of monomeric human interleukin-8 (minimized average structure)==
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|PDB= 1ikl |SIZE=350|CAPTION= <scene name='initialview01'>1ikl</scene>
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<StructureSection load='1ikl' size='340' side='right'caption='[[1ikl]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=CH3:METHYL+GROUP'>CH3</scene>
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<table><tr><td colspan='2'>[[1ikl]] 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=1IKL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IKL FirstGlance]. <br>
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|ACTIVITY=
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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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|GENE=
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MLE:N-METHYLLEUCINE'>MLE</scene></td></tr>
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|DOMAIN=
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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=1ikl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ikl OCA], [https://pdbe.org/1ikl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ikl RCSB], [https://www.ebi.ac.uk/pdbsum/1ikl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ikl ProSAT]</span></td></tr>
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|RELATEDENTRY=[[1ikm|1IKM]]
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</table>
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ikl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ikl OCA], [http://www.ebi.ac.uk/pdbsum/1ikl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ikl RCSB]</span>
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== Function ==
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}}
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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/ik/1ikl_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=1ikl ConSurf].
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<div style="clear:both"></div>
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'''NMR STUDY OF MONOMERIC HUMAN INTERLEUKIN-8 (MINIMIZED AVERAGE STRUCTURE)'''
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==See Also==
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*[[Interleukin 3D structures|Interleukin 3D structures]]
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== References ==
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==Overview==
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<references/>
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The solution structure of a monomeric form of interleukin-8 (IL-8) has been solved using 1H NMR spectroscopy. The chemically synthesized nonnatural analog [IL-8 (4-72) L25 NH--&gt;NCH3] has the same activity as that of native IL-8. Thirty structures were generated using the hybrid distance geometry and simulated annealing protocol using the program X-PLOR. The structure is well-defined except for N-terminal residues 4-6 and C-terminal residues 67-72. The rms distribution about the average structure for residues 7-66 is 0.38 A for the backbone atoms and 0.87 A for all heavy atoms. The structure consists of a series of turns and loops followed by a triple-stranded beta sheet and a C-terminal alpha helix. The structure of the monomer is largely similar to the native dimeric IL-8 structures previously determined by both NMR and X-ray methods. The major difference is that, in the monomeric analog, the C-terminal residues 67-72 are disordered whereas they are helical in the two dimeric structures. The best fit superposition of the backbone atoms of residues 7-66 of the monomer structure on the dimeric IL-8 structures showed rms differences of 1.5 and 1.2 A respectively. The turn (residues 31-35), which is disulfide linked to the N-terminal region, adopts a conformation in the monomer similar to that seen in the dimeric X-ray structure (rms difference 1.4 A) and different from that seen in the dimeric NMR structure (rms difference 2.7 A).(ABSTRACT TRUNCATED AT 250 WORDS)
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__TOC__
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</StructureSection>
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==About this Structure==
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1IKL is a [[Single protein]] structure of 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=1IKL OCA].
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==Reference==
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1H NMR solution structure of an active monomeric interleukin-8., Rajarathnam K, Clark-Lewis I, Sykes BD, Biochemistry. 1995 Oct 10;34(40):12983-90. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7548056 7548056]
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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: Clark-Lewis, I.]]
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[[Category: Clark-Lewis I]]
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[[Category: Rajarathnam, K.]]
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[[Category: Rajarathnam K]]
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[[Category: Sykes, B D.]]
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[[Category: Sykes BD]]
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[[Category: cytokine (chemotactic)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:21:03 2008''
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NMR study of monomeric human interleukin-8 (minimized average structure)

PDB ID 1ikl

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