1i6z: Difference between revisions

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 ==BAG DOMAIN OF BAG1 COCHAPERONE==
-<StructureSection load='1i6z' size='340' side='right'caption='[[1i6z]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''>
+<StructureSection load='1i6z' size='340' side='right'caption='[[1i6z]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1i6z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I6Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I6Z FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1i6z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1I6Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I6Z FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BAG1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1i6z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i6z OCA], [https://pdbe.org/1i6z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i6z RCSB], [https://www.ebi.ac.uk/pdbsum/1i6z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i6z ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/BAG1_MOUSE BAG1_MOUSE]] Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. Inhibits the pro-apoptotic function of PPP1R15A, and has anti-apoptotic activity. Markedly increases the anti-cell death function of BCL2 induced by various stimuli.<ref>PMID:9873016</ref>
+[https://www.uniprot.org/uniprot/BAG1_MOUSE BAG1_MOUSE] Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release. Inhibits the pro-apoptotic function of PPP1R15A, and has anti-apoptotic activity. Markedly increases the anti-cell death function of BCL2 induced by various stimuli.<ref>PMID:9873016</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 19: / Line 19: @@
 </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=1i6z ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-BAG-family proteins share a conserved protein interaction region, called the 'BAG domain', which binds and regulates Hsp70/Hsc70 molecular chaperones. This family of cochaperones functionally regulates signal transducing proteins and transcription factors important for cell stress responses, apoptosis, proliferation, cell migration and hormone action. Aberrant overexpression of the founding member of this family, BAG1, occurs in human cancers. In this study, a structure-based approach was used to identify interacting residues in a BAG1--Hsc70 complex. An Hsc70-binding fragment of BAG1 was shown by multidimensional NMR methods to consist of an antiparallel three-helix bundle. NMR chemical shift experiments marked surface residues on the second (alpha 2) and third (alpha 3) helices in the BAG domain that are involved in chaperone binding. Structural predictions were confirmed by site-directed mutagenesis of these residues, resulting in loss of binding of BAG1 to Hsc70 in vitro and in cells. Molecular docking of BAG1 to Hsc70 and mutagenesis of Hsc70 marked the molecular surface of the ATPase domain necessary for interaction with BAG1. The results provide a structural basis for understanding the mechanism by which BAG proteins link molecular chaperones and cell signaling pathways.
-Structural analysis of BAG1 cochaperone and its interactions with Hsc70 heat shock protein.,Briknarova K, Takayama S, Brive L, Havert ML, Knee DA, Velasco J, Homma S, Cabezas E, Stuart J, Hoyt DW, Satterthwait AC, Llinas M, Reed JC, Ely KR Nat Struct Biol. 2001 Apr;8(4):349-52. PMID:11276257<ref>PMID:11276257</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1i6z" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 36: / Line 27: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Lk3 transgenic mice]]
+[[Category: Mus musculus]]
-[[Category: Briknarova, K]]
+[[Category: Briknarova K]]
-[[Category: Brive, L]]
+[[Category: Brive L]]
-[[Category: Cabezas, E]]
+[[Category: Cabezas E]]
-[[Category: Ely, K R]]
+[[Category: Ely KR]]
-[[Category: Havert, M L]]
+[[Category: Havert ML]]
-[[Category: Homma, S]]
+[[Category: Homma S]]
-[[Category: Hoyt, D W]]
+[[Category: Hoyt DW]]
-[[Category: Knee, D A]]
+[[Category: Knee DA]]
-[[Category: Llinas, M]]
+[[Category: Llinas M]]
-[[Category: Reed, J C]]
+[[Category: Reed JC]]
-[[Category: Satterthwait, A C]]
+[[Category: Satterthwait AC]]
-[[Category: Stuart, J]]
+[[Category: Stuart J]]
-[[Category: Takayama, S]]
+[[Category: Takayama S]]
-[[Category: Velasco, J]]
+[[Category: Velasco J]]
-[[Category: Chaperone]]
-[[Category: Triple helix bundle]]