1m62

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[[Image:1m62.gif|left|200px]]
 
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{{Structure
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==Solution structure of the BAG domain from BAG4/SODD==
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|PDB= 1m62 |SIZE=350|CAPTION= <scene name='initialview01'>1m62</scene>
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<StructureSection load='1m62' size='340' side='right'caption='[[1m62]]' 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'>[[1m62]] 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=1M62 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M62 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= BAG4/SODD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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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=1m62 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m62 OCA], [https://pdbe.org/1m62 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m62 RCSB], [https://www.ebi.ac.uk/pdbsum/1m62 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m62 ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=[[1i6z|1I6Z]], [[1hx1|1HX1]]
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m62 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m62 OCA], [http://www.ebi.ac.uk/pdbsum/1m62 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1m62 RCSB]</span>
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[https://www.uniprot.org/uniprot/BAG4_HUMAN BAG4_HUMAN] Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release (By similarity). Prevents constitutive TNFRSF1A signaling.
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}}
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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/m6/1m62_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=1m62 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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BAG (Bcl-2-associated athanogene) proteins are molecular chaperone regulators that affect diverse cellular pathways. All members share a conserved motif, called the BAG domain (BD), which binds to Hsp70/Hsc70 family proteins and modulates their activity. We have determined the solution structure of BD from BAG4/SODD (silencer of death domains) by multidimensional nuclear magnetic resonance methods and compared it to the corresponding domain in BAG1 (Briknarova, K., Takayama, S., Brive, L., Havert, M. L., Knee, D. A., Velasco, J., Homma, S., Cabezas, E., Stuart, J., Hoyt, D. W., Satterthwait, A. C., Llinas, M., Reed, J. C., and Ely, K. R. (2001) Nat. Struct. Biol. 8, 349-352). The difference between BDs from these two BAG proteins is striking, and the structural comparison defines two subfamilies of mammalian BD-containing proteins. One subfamily includes the closely related BAG3, BAG4, and BAG5 proteins, and the other is represented by BAG1, which contains a structurally and evolutionarily distinct BD. BDs from both BAG1 and BAG4 are three-helix bundles; however, in BAG4, each helix in this bundle is three to four turns shorter than its counterpart in BAG1, which reduces the length of the domain by one-third. BAG4 BD thus represents a prototype of the minimal functional fragment that is capable of binding to Hsc70 and modulating its chaperone activity.
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'''Solution structure of the BAG domain from BAG4/SODD'''
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BAG4/SODD protein contains a short BAG domain.,Briknarova K, Takayama S, Homma S, Baker K, Cabezas E, Hoyt DW, Li Z, Satterthwait AC, Ely KR J Biol Chem. 2002 Aug 23;277(34):31172-8. Epub 2002 Jun 10. PMID:12058034<ref>PMID:12058034</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 1m62" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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BAG (Bcl-2-associated athanogene) proteins are molecular chaperone regulators that affect diverse cellular pathways. All members share a conserved motif, called the BAG domain (BD), which binds to Hsp70/Hsc70 family proteins and modulates their activity. We have determined the solution structure of BD from BAG4/SODD (silencer of death domains) by multidimensional nuclear magnetic resonance methods and compared it to the corresponding domain in BAG1 (Briknarova, K., Takayama, S., Brive, L., Havert, M. L., Knee, D. A., Velasco, J., Homma, S., Cabezas, E., Stuart, J., Hoyt, D. W., Satterthwait, A. C., Llinas, M., Reed, J. C., and Ely, K. R. (2001) Nat. Struct. Biol. 8, 349-352). The difference between BDs from these two BAG proteins is striking, and the structural comparison defines two subfamilies of mammalian BD-containing proteins. One subfamily includes the closely related BAG3, BAG4, and BAG5 proteins, and the other is represented by BAG1, which contains a structurally and evolutionarily distinct BD. BDs from both BAG1 and BAG4 are three-helix bundles; however, in BAG4, each helix in this bundle is three to four turns shorter than its counterpart in BAG1, which reduces the length of the domain by one-third. BAG4 BD thus represents a prototype of the minimal functional fragment that is capable of binding to Hsc70 and modulating its chaperone activity.
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*[[BAG family proteins 3D structures|BAG family proteins 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1M62 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=1M62 OCA].
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__TOC__
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</StructureSection>
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==Reference==
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BAG4/SODD protein contains a short BAG domain., Briknarova K, Takayama S, Homma S, Baker K, Cabezas E, Hoyt DW, Li Z, Satterthwait AC, Ely KR, J Biol Chem. 2002 Aug 23;277(34):31172-8. Epub 2002 Jun 10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12058034 12058034]
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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: Baker, K.]]
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[[Category: Baker K]]
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[[Category: Briknarova, K.]]
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[[Category: Briknarova K]]
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[[Category: Cabezas, E.]]
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[[Category: Cabezas E]]
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[[Category: Ely, K R.]]
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[[Category: Ely KR]]
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[[Category: Homma, S.]]
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[[Category: Homma S]]
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[[Category: Hoyt, D W.]]
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[[Category: Hoyt DW]]
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[[Category: Li, Z.]]
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[[Category: Li Z]]
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[[Category: Satterthwait, A C.]]
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[[Category: Satterthwait AC]]
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[[Category: Takayama, S.]]
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[[Category: Takayama S]]
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[[Category: bag domain]]
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[[Category: bag4]]
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[[Category: hsp70/hsc70 co-chaperone]]
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[[Category: silencer of death domain]]
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[[Category: sodd]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:11:51 2008''
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Current revision

Solution structure of the BAG domain from BAG4/SODD

PDB ID 1m62

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