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1irl

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[[Image:1irl.gif|left|200px]]
 
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{{Structure
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==THE SOLUTION STRUCTURE OF THE F42A MUTANT OF HUMAN INTERLEUKIN 2==
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|PDB= 1irl |SIZE=350|CAPTION= <scene name='initialview01'>1irl</scene>
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<StructureSection load='1irl' size='340' side='right'caption='[[1irl]]' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1irl]] 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=1IRL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IRL 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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1irl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1irl OCA], [https://pdbe.org/1irl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1irl RCSB], [https://www.ebi.ac.uk/pdbsum/1irl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1irl ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Disease ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1irl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1irl OCA], [http://www.ebi.ac.uk/pdbsum/1irl PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1irl RCSB]</span>
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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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}}
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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/ir/1irl_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=1irl ConSurf].
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<div style="clear:both"></div>
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'''THE SOLUTION STRUCTURE OF THE F42A MUTANT OF HUMAN INTERLEUKIN 2'''
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==See Also==
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*[[Interleukin 3D structures|Interleukin 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Interleukin 2 (IL-2) is one of the major cytokines produced by T lymphocytes in response to antigen. It is a potent growth and differentiation factor for several cell-types and is structurally related to the four-helix bundle family of cytokines. Mutation of residue Phe42 to Ala abolishes binding to the alpha chain of the tri-partite IL-2 receptor. The three-dimensional structure of the F42A mutant IL-2 has been calculated by two dimensional NMR methods and compared to a structure of wild-type IL-2 determined by X-ray crystallography. The overall topology of the two structures is the same. The main differences between the structures are within the ill-defined loops connecting the helices and the region of the protein that is believed to interact with the alpha-chain of the receptor. Thus, the mutation of Phe42 to Ala does not perturb the overall three-dimensional structure of IL-2, and does not appear to change the putative binding sites for the beta and gamma chains of the receptor. The structural differences observed in this mutant suggest that the replacement of Phe42 with Ala causes the re-orientation of neighbouring side-chains that are also involved in binding the alpha-chain of the receptor.
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==About this Structure==
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1IRL 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=1IRL OCA].
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==Reference==
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The solution structure of the F42A mutant of human interleukin 2., Mott HR, Baines BS, Hall RM, Cooke RM, Driscoll PC, Weir MP, Campbell ID, J Mol Biol. 1995 Apr 14;247(5):979-94. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7723044 7723044]
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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: Baines, B S.]]
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[[Category: Baines BS]]
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[[Category: Campbell, I D.]]
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[[Category: Campbell ID]]
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[[Category: Cooke, R M.]]
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[[Category: Cooke RM]]
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[[Category: Driscoll, P C.]]
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[[Category: Driscoll PC]]
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[[Category: Hall, R M.]]
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[[Category: Hall RM]]
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[[Category: Mott, H R.]]
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[[Category: Mott HR]]
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[[Category: Weir, M P.]]
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[[Category: Weir MP]]
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[[Category: cytokine]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:23:40 2008''
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Current revision

THE SOLUTION STRUCTURE OF THE F42A MUTANT OF HUMAN INTERLEUKIN 2

PDB ID 1irl

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