3m9j

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{{Seed}}
 
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[[Image:3m9j.png|left|200px]]
 
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==Crystal structure of human thioredoxin C69/73S double mutant, reduced form==
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The line below this paragraph, containing "STRUCTURE_3m9j", creates the "Structure Box" on the page.
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<StructureSection load='3m9j' size='340' side='right'caption='[[3m9j]], [[Resolution|resolution]] 1.10&Aring;' scene=''>
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3m9j]] is a 2 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=3M9J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3M9J 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]] 1.1&#8491;</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=3m9j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3m9j OCA], [https://pdbe.org/3m9j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3m9j RCSB], [https://www.ebi.ac.uk/pdbsum/3m9j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3m9j ProSAT]</span></td></tr>
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{{STRUCTURE_3m9j| PDB=3m9j | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/THIO_HUMAN THIO_HUMAN] Participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyzes dithiol-disulfide exchange reactions. Plays a role in the reversible S-nitrosylation of cysteine residues in target proteins, and thereby contributes to the response to intracellular nitric oxide. Nitrosylates the active site Cys of CASP3 in response to nitric oxide (NO), and thereby inhibits caspase-3 activity. Induces the FOS/JUN AP-1 DNA-binding activity in ionizing radiation (IR) cells through its oxidation/reduction status and stimulates AP-1 transcriptional activity.<ref>PMID:2176490</ref> <ref>PMID:9108029</ref> <ref>PMID:11118054</ref> <ref>PMID:16408020</ref> <ref>PMID:17606900</ref> ADF augments the expression of the interleukin-2 receptor TAC (IL2R/P55).<ref>PMID:2176490</ref> <ref>PMID:9108029</ref> <ref>PMID:11118054</ref> <ref>PMID:16408020</ref> <ref>PMID:17606900</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/m9/3m9j_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=3m9j 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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Thioredoxins reduce disulfide bonds and other thiol modifications in all cells, using a CXXC motif. Human thioredoxin 1 is unusual in that it codes for an additional three cysteines in its 105 amino acid sequence, each of which have been implicated in other reductive activities. Cys 62 and Cys 69 are buried in the protein interior and lie at either end of a short helix (helix 3), and yet can disulfide link under oxidizing conditions. Cys 62 is readily S-nitrosated, giving rise to a SNO modification, which is also buried. Here, we present two crystal structures of the C69S/C73S mutant protein under oxidizing (1.5 A) and reducing (1.1 A) conditions. In the oxidized structure, helix 3 is unraveled and displays a new conformation that is stabilized by a series of new hydrogen bonds and a disulfide link with Cys 62 in a neighboring molecule. The new conformation provides an explanation for how a completely buried residue can participate in SNO exchange reactions.
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===Crystal structure of human thioredoxin C69/73S double mutant, reduced form===
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Crystal structure of human thioredoxin revealing an unraveled helix and exposed S- nitrosation site.,Weichsel A, Kem M, Montfort WR Protein Sci. 2010 Jul 26. PMID:20662007<ref>PMID:20662007</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3m9j" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_20662007}}, adds the Publication Abstract to the page
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*[[Thioredoxin 3D structures|Thioredoxin 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 20662007 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_20662007}}
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__TOC__
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</StructureSection>
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==About this Structure==
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3M9J is a 2 chains structure with sequences 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=3M9J OCA].
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==Reference==
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<ref group="xtra">PMID:20662007</ref><ref group="xtra">PMID:17260951</ref><ref group="xtra">PMID:8805557</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Montfort, W R.]]
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[[Category: Large Structures]]
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[[Category: Weichsel, A.]]
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[[Category: Montfort WR]]
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[[Category: Oxidoreductase]]
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[[Category: Weichsel A]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Dec 8 11:17:10 2010''
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Current revision

Crystal structure of human thioredoxin C69/73S double mutant, reduced form

PDB ID 3m9j

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