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==Solution Structure of the SODD BAG Domain== | |||
<StructureSection load='1m7k' size='340' side='right'caption='[[1m7k]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1m7k]] 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=1M7K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M7K FirstGlance]. <br> | |||
</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=1m7k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m7k OCA], [https://pdbe.org/1m7k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m7k RCSB], [https://www.ebi.ac.uk/pdbsum/1m7k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m7k ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[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. | |||
== 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/m7/1m7k_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=1m7k ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The solution structure of an N-terminally extended construct of the SODD BAG domain was determined by nuclear magnetic resonance spectroscopy. A homology model of the SODD-BAG/HSP70 complex reveals additional possible interactions that are specific for the SODD subfamily of BAG domains while the overall geometry of the complex remains the same. Relaxation rate measurements show that amino acids N358-S375 of SODD which were previously assigned to its BAG domain are not structured in our construct. The SODD BAG domain is thus indeed smaller than the homologous domain in Bag1 defining a new subfamily of BAG domains. | |||
The solution structure of the SODD BAG domain reveals additional electrostatic interactions in the HSP70 complexes of SODD subfamily BAG domains.,Brockmann C, Leitner D, Labudde D, Diehl A, Sievert V, Bussow K, Kuhne R, Oschkinat H FEBS Lett. 2004 Jan 30;558(1-3):101-6. PMID:14759524<ref>PMID:14759524</ref> | |||
The solution structure | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1m7k" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[BAG family proteins 3D structures|BAG family proteins 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Brockmann | [[Category: Brockmann C]] | ||
[[Category: Buessow | [[Category: Buessow K]] | ||
[[Category: Diehl | [[Category: Diehl A]] | ||
[[Category: Labudde | [[Category: Labudde D]] | ||
[[Category: Leitner | [[Category: Leitner D]] | ||
[[Category: Oschkinat | [[Category: Oschkinat H]] | ||
[[Category: Sievert | [[Category: Sievert V]] | ||
Latest revision as of 21:13, 29 May 2024
Solution Structure of the SODD BAG DomainSolution Structure of the SODD BAG Domain
Structural highlights
FunctionBAG4_HUMAN Inhibits the chaperone activity of HSP70/HSC70 by promoting substrate release (By similarity). Prevents constitutive TNFRSF1A signaling. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe solution structure of an N-terminally extended construct of the SODD BAG domain was determined by nuclear magnetic resonance spectroscopy. A homology model of the SODD-BAG/HSP70 complex reveals additional possible interactions that are specific for the SODD subfamily of BAG domains while the overall geometry of the complex remains the same. Relaxation rate measurements show that amino acids N358-S375 of SODD which were previously assigned to its BAG domain are not structured in our construct. The SODD BAG domain is thus indeed smaller than the homologous domain in Bag1 defining a new subfamily of BAG domains. The solution structure of the SODD BAG domain reveals additional electrostatic interactions in the HSP70 complexes of SODD subfamily BAG domains.,Brockmann C, Leitner D, Labudde D, Diehl A, Sievert V, Bussow K, Kuhne R, Oschkinat H FEBS Lett. 2004 Jan 30;558(1-3):101-6. PMID:14759524[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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