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1qe6

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(New page: 200px<br /> <applet load="1qe6" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qe6, resolution 2.35&Aring;" /> '''INTERLEUKIN-8 WITH ...)
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[[Image:1qe6.gif|left|200px]]<br />
 
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<applet load="1qe6" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1qe6, resolution 2.35&Aring;" />
 
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'''INTERLEUKIN-8 WITH AN ADDED DISULFIDE BETWEEN RESIDUES 5 AND 33 (L5C/H33C)'''<br />
 
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==Overview==
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==INTERLEUKIN-8 WITH AN ADDED DISULFIDE BETWEEN RESIDUES 5 AND 33 (L5C/H33C)==
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The "ELR" (Glu-Leu-Arg) tripeptide sequence near the N-terminus of, interleukin-8 (IL-8) contributes a large part of the receptor binding free, energy. Prior X-ray and nuclear magnetic resonance (NMR) structures of, IL-8 have shown this region of the molecule to be highly mobile. We, reasoned that a hydrophobic interaction between the leucine and the, neighboring beta-turn might exist in the receptor binding conformation of, the N-terminus. To test this hypothesis, we mutated two residues to, cysteine and connected the N-terminus to the beta-turn. The mutant retains, receptor binding affinity reasonably close to wild type and allows the, characterization of a high-affinity conformation that may be useful in the, design of small IL-8 mimics. The L5C/H33C mutant is refined to R-values of, R = 20.6% and Rfree = 27.7% at 2.35 A resolution. Other receptor binding, determinants reside in the "N-loop" found after "ELR" and preceding the, first beta-strand. All available structures of IL-8 have been found with, one of two distinct N-loop conformations. One of these is relevant for, receptor binding, based on NMR results with receptor peptides. The other, conformation obscures the receptor-peptide binding surface and may have an, undetermined but necessarily different function.
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<StructureSection load='1qe6' size='340' side='right'caption='[[1qe6]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1qe6]] is a 4 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=1QE6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QE6 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">X-ray diffraction, [[Resolution|Resolution]] 2.35&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1qe6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qe6 OCA], [https://pdbe.org/1qe6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qe6 RCSB], [https://www.ebi.ac.uk/pdbsum/1qe6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qe6 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/qe/1qe6_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=1qe6 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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1QE6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QE6 OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Receptor-binding conformation of the "ELR" motif of IL-8: X-ray structure of the L5C/H33C variant at 2.35 A resolution., Gerber N, Lowman H, Artis DR, Eigenbrot C, Proteins. 2000 Mar 1;38(4):361-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10707023 10707023]
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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: Artis, D.R.]]
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[[Category: Artis DR]]
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[[Category: Eigenbrot, C.]]
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[[Category: Eigenbrot C]]
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[[Category: Gerber, N.]]
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[[Category: Gerber N]]
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[[Category: Lowman, H.]]
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[[Category: Lowman H]]
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[[Category: SO4]]
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[[Category: intercrine alpha family]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:52:32 2007''
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Current revision

INTERLEUKIN-8 WITH AN ADDED DISULFIDE BETWEEN RESIDUES 5 AND 33 (L5C/H33C)

PDB ID 1qe6

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