2gto

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[[Image:2gto.png|left|200px]]
 
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==Oxidized form of ADAP hSH3-N==
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The line below this paragraph, containing "STRUCTURE_2gto", creates the "Structure Box" on the page.
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<StructureSection load='2gto' size='340' side='right'caption='[[2gto]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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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'>[[2gto]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GTO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GTO FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2gtj|2gtj]]</div></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FYB, SLAP130 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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{{STRUCTURE_2gto| PDB=2gto | SCENE= }}
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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=2gto FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gto OCA], [https://pdbe.org/2gto PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2gto RCSB], [https://www.ebi.ac.uk/pdbsum/2gto PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2gto ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[https://www.uniprot.org/uniprot/FYB_HUMAN FYB_HUMAN]] Acts as an adapter protein of the FYN and LCP2 signaling cascades in T-cells. Modulates the expression of interleukin-2 (IL-2). Involved in platelet activation. Prevents the degradation of SKAP1 and SKAP2. May play a role in linking T-cell signaling to remodeling of the actin cytoskeleton.<ref>PMID:10747096</ref> <ref>PMID:15849195</ref> <ref>PMID:16980616</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/gt/2gto_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=2gto 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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Oxidation-induced conformational changes in proteins provide a powerful mechanism to sense the redox state of a living cell. In contrast to the unspecific and often irreversible oxidation of intracellular proteins during severe oxidative stress, regulatory redox events need to have specific and transient effects on cellular targets. Here we present evidence for the reversible formation of a vicinal disulfide bond in a prototypic protein interaction domain. NMR spectroscopy was used to determine the structure of the N-terminal hSH3 domain (hSH3N) of the immune cell protein ADAP (adhesion and degranulation promoting adapter protein) in the reduced and oxidized states. An eight-membered ring formed upon oxidation of two neighboring cysteines leads to significant changes in the variable arginine-threonine (RT) loop of the hSH3N domain and alters the helix-sheet packing of the domain. The redox potential for this structural transition is -228 mV at pH 7.4. This is compatible with a role of the cysteinylcysteine moiety in redox signaling during T cell activation.
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===Oxidized form of ADAP hSH3-N===
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Redox-regulated conformational changes in an SH3 domain.,Zimmermann J, Kuhne R, Sylvester M, Freund C Biochemistry. 2007 Jun 12;46(23):6971-7. Epub 2007 May 19. PMID:17511475<ref>PMID:17511475</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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The line below this paragraph, {{ABSTRACT_PUBMED_17511475}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2gto" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 17511475 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_17511475}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Human]]
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[[2gto]] is a 1 chain structure with sequence 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=2GTO OCA].
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[[Category: Large Structures]]
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[[Category: Freund, C]]
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==Reference==
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[[Category: Kuehne, R]]
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<ref group="xtra">PMID:17511475</ref><ref group="xtra">PMID:16041492</ref><references group="xtra"/>
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[[Category: Zimmermann, J]]
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[[Category: Homo sapiens]]
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[[Category: Freund, C.]]
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[[Category: Kuehne, R.]]
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[[Category: Zimmermann, J.]]
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[[Category: Signaling protein]]
[[Category: Signaling protein]]

Current revision

Oxidized form of ADAP hSH3-N

PDB ID 2gto

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