2gto: Difference between revisions

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OCA

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-[[Image:2gto.gif|left|200px]]<br />
-<applet load="2gto" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="2gto" />
-'''Oxidized form of ADAP hSH3-N'''<br />
-==Overview==
+==Oxidized form of ADAP hSH3-N==
-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.
+<StructureSection load='2gto' size='340' side='right'caption='[[2gto]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+== Structural highlights ==
+<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>
+</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>
+<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>
+<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>
+</table>
+== Function ==
+[[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>
+== 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/gt/2gto_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=2gto ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-==About this Structure==
+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>
-GTO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2GTO OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17511475 17511475]
+</div>
-[[Category: Homo sapiens]]
+<div class="pdbe-citations 2gto" style="background-color:#fffaf0;"></div>
-[[Category: Single protein]]
+== References ==
-[[Category: Freund, C.]]
+<references/>
-[[Category: Kuehne, R.]]
+__TOC__
-[[Category: Zimmermann, J.]]
+</StructureSection>
-[[Category: helically extended sh3 domain (hsh3)]]
+[[Category: Human]]
+[[Category: Large Structures]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:22:38 2007''
+[[Category: Freund, C]]
+[[Category: Kuehne, R]]
+[[Category: Zimmermann, J]]
+[[Category: Signaling protein]]