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1nbp

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(New page: 200px<br /> <applet load="1nbp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nbp, resolution 2.20&Aring;" /> '''Crystal Structure O...)
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[[Image:1nbp.gif|left|200px]]<br />
 
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<applet load="1nbp" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1nbp, resolution 2.20&Aring;" />
 
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'''Crystal Structure Of Human Interleukin-2 Y31C Covalently Modified At C31 With 3-Mercapto-1-(1,3,4,9-tetrahydro-B-carbolin-2-yl)-propan-1-one'''<br />
 
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==Overview==
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==Crystal Structure Of Human Interleukin-2 Y31C Covalently Modified At C31 With 3-Mercapto-1-(1,3,4,9-tetrahydro-B-carbolin-2-yl)-propan-1-one==
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The cytokine hormone interleukin-2 (IL-2) contains a highly adaptive, region that binds small, druglike molecules. The binding properties of, this adaptive region have been explored using a "tethering" method that, relies on the formation of a disulfide bond between the protein and, small-molecule ligands. Using tethering, surface plasmon resonance (SPR), and X-ray crystallography, we have discovered that the IL-2 adaptive, region contains at least two cooperative binding sites where the binding, of a first ligand to one site promotes or antagonizes the binding of a, second ligand to the second site. Cooperative energies of interaction of, -2 kcal/mol are observed. The observation that the adaptive region, contains two adjacent sites may lead to the development of tight-binding, antagonists of a protein-protein interaction. Cooperative ligand binding, in the adaptive region of IL-2 underscores the importance of protein, dynamics in molecular recognition. The tethering approach provides a novel, and general strategy for discovering such cooperative binding interactions, in specific, flexible regions of protein structure.
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<StructureSection load='1nbp' size='340' side='right'caption='[[1nbp]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1nbp]] is a 1 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=1NBP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NBP 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]] 2.2&#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=MHC:3-MERCAPTO-1-(1,3,4,9-TETRAHYDRO-B-CARBOLIN-2-YL)-PROPAN-1-ONE'>MHC</scene>, <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=1nbp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nbp OCA], [https://pdbe.org/1nbp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nbp RCSB], [https://www.ebi.ac.uk/pdbsum/1nbp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nbp ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/IL2_HUMAN IL2_HUMAN] Note=A chromosomal aberration involving IL2 is found in a form of T-cell acute lymphoblastic leukemia (T-ALL). Translocation t(4;16)(q26;p13) with involves TNFRSF17.
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== Function ==
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[https://www.uniprot.org/uniprot/IL2_HUMAN IL2_HUMAN] Produced by T-cells in response to antigenic or mitogenic stimulation, this protein is required for T-cell proliferation and other activities crucial to regulation of the immune response. Can stimulate B-cells, monocytes, lymphokine-activated killer cells, natural killer cells, and glioma cells.
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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/nb/1nbp_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=1nbp ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The cytokine hormone interleukin-2 (IL-2) contains a highly adaptive region that binds small, druglike molecules. The binding properties of this adaptive region have been explored using a "tethering" method that relies on the formation of a disulfide bond between the protein and small-molecule ligands. Using tethering, surface plasmon resonance (SPR), and X-ray crystallography, we have discovered that the IL-2 adaptive region contains at least two cooperative binding sites where the binding of a first ligand to one site promotes or antagonizes the binding of a second ligand to the second site. Cooperative energies of interaction of -2 kcal/mol are observed. The observation that the adaptive region contains two adjacent sites may lead to the development of tight-binding antagonists of a protein-protein interaction. Cooperative ligand binding in the adaptive region of IL-2 underscores the importance of protein dynamics in molecular recognition. The tethering approach provides a novel and general strategy for discovering such cooperative binding interactions in specific, flexible regions of protein structure.
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==Disease==
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Discovery and characterization of cooperative ligand binding in the adaptive region of interleukin-2.,Hyde J, Braisted AC, Randal M, Arkin MR Biochemistry. 2003 Jun 3;42(21):6475-83. PMID:12767230<ref>PMID:12767230</ref>
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Known disease associated with this structure: Severe combined immunodeficiency due to IL2 deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=147680 147680]]
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==About this Structure==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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1NBP 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 and MHC as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NBP OCA].
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</div>
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<div class="pdbe-citations 1nbp" style="background-color:#fffaf0;"></div>
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==Reference==
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==See Also==
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Discovery and characterization of cooperative ligand binding in the adaptive region of interleukin-2., Hyde J, Braisted AC, Randal M, Arkin MR, Biochemistry. 2003 Jun 3;42(21):6475-83. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12767230 12767230]
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*[[Interleukin 3D structures|Interleukin 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[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: Arkin, M.R.]]
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[[Category: Arkin MR]]
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[[Category: Braisted, A.C.]]
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[[Category: Braisted AC]]
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[[Category: Hyde, J.]]
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[[Category: Hyde J]]
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[[Category: Randal, M.]]
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[[Category: Randal M]]
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[[Category: MHC]]
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[[Category: SO4]]
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[[Category: cytokine]]
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[[Category: four-helix bundle]]
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[[Category: small molecule complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:20:16 2007''
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Current revision

Crystal Structure Of Human Interleukin-2 Y31C Covalently Modified At C31 With 3-Mercapto-1-(1,3,4,9-tetrahydro-B-carbolin-2-yl)-propan-1-one

PDB ID 1nbp

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