1rod: Difference between revisions

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-{{Seed}}
-[[Image:1rod.png|left|200px]]
-<!--
+==CHIMERIC PROTEIN OF INTERLEUKIN 8 AND HUMAN MELANOMA GROWTH STIMULATING ACTIVITY PROTEIN, NMR==
-The line below this paragraph, containing "STRUCTURE_1rod", creates the "Structure Box" on the page.
+<StructureSection load='1rod' size='340' side='right'caption='[[1rod]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1rod]] 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=1ROD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ROD FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 8 models</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=1rod FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rod OCA], [https://pdbe.org/1rod PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rod RCSB], [https://www.ebi.ac.uk/pdbsum/1rod PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rod ProSAT]</span></td></tr>
-{{STRUCTURE_1rod|  PDB=1rod  |  SCENE=  }}
+</table>
+== Function ==
+[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>
+== 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/ro/1rod_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=1rod ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+A 72-amino-acid chimeric protein, Chi1, was constructed from the N-terminal part of interleukin 8, IL-8-(1-53), and the C-terminal part of melanoma growth stimulatory activity, MGSA-(54-72). Chi1 protein showed receptor-binding specificity and biological activity similar, but not identical to IL-8 and decidedly different from MGSA. The structure of Chi1 was determined in solution by two-dimensional NMR and molecular-dynamics calculations. The structure resembled the structures of MGSA and IL-8 closely, containing a triple-stranded beta-sheet in the IL-8 part and an amphipathic alpha-helix in the MGSA part. Chi1 formed dimers at millimolar concentrations via the first strand from the N-terminus, analogous to IL-8 and MGSA. In contrast to the latter molecules, however, the alpha-helix of Chi1 did not pack against the beta-sheet part, but was an independent structural element. This structural difference could be explained mainly by the modulation of hydrophobic interactions between the helix and the rest of the protein in Chi1 as compared to IL-8 and MGSA. It is concluded that tight helix packing is not required for receptor binding and biological activity of Chi1.
-===CHIMERIC PROTEIN OF INTERLEUKIN 8 AND HUMAN MELANOMA GROWTH STIMULATING ACTIVITY PROTEIN, NMR===
+Structure and activity of a chimeric interleukin-8-melanoma-growth-stimulatory-activity protein.,Sticht H, Auer M, Schmitt B, Besemer J, Horcher M, Kirsch T, Lindley IJ, Rosch P Eur J Biochem. 1996 Jan 15;235(1-2):26-35. PMID:8631339<ref>PMID:8631339</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1rod" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_8631339}}, adds the Publication Abstract to the page
+*[[Interleukin 3D structures|Interleukin 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 8631339 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_8631339}}
+__TOC__
+</StructureSection>
-==About this Structure==
-ROD is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ROD OCA].
-==Reference==
-<ref group="xtra">PMID:8631339</ref><references group="xtra"/>
 [[Category: Homo sapiens]]
-[[Category: Auer, M.]]
+[[Category: Large Structures]]
-[[Category: Besemer, J.]]
+[[Category: Auer M]]
-[[Category: Horcher, M.]]
+[[Category: Besemer J]]
-[[Category: Kirsch, T.]]
+[[Category: Horcher M]]
-[[Category: Lindley, I J.D.]]
+[[Category: Kirsch T]]
-[[Category: Roesch, P.]]
+[[Category: Lindley IJD]]
-[[Category: Schmitt, B.]]
+[[Category: Roesch P]]
-[[Category: Sticht, H.]]
+[[Category: Schmitt B]]
-[[Category: Chemokine]]
+[[Category: Sticht H]]
-[[Category: Chemotaxis]]
-[[Category: Cytokine]]
-[[Category: Inflammatory response]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 19:50:04 2009''