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1m62

From Proteopedia

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Current revision

Solution structure of the BAG domain from BAG4/SODD

Structural highlights

1m62 is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BAG4_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 PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Briknarova K, Takayama S, Homma S, Baker K, Cabezas E, Hoyt DW, Li Z, Satterthwait AC, Ely KR. BAG4/SODD protein contains a short BAG domain. J Biol Chem. 2002 Aug 23;277(34):31172-8. Epub 2002 Jun 10. PMID:12058034 doi:10.1074/jbc.M202792200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1m62"

@@ Line 1: / Line 1: @@
 ==Solution structure of the BAG domain from BAG4/SODD==
-<StructureSection load='1m62' size='340' side='right'caption='[[1m62]], [[NMR_Ensembles_of_Models | 25 NMR models]]' scene=''>
+<StructureSection load='1m62' size='340' side='right'caption='[[1m62]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1m62]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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 [http://proteopedia.org/fgij/fg.htm?mol=1M62 FirstGlance]. <br>
+<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>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1i6z|1i6z]], [[1hx1|1hx1]]</div></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BAG4/SODD ([http://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=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>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1m62 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m62 OCA], [http://pdbe.org/1m62 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1m62 RCSB], [http://www.ebi.ac.uk/pdbsum/1m62 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1m62 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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.
+[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]]
@@ Line 36: / Line 35: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Baker, K]]
+[[Category: Baker K]]
-[[Category: Briknarova, K]]
+[[Category: Briknarova K]]
-[[Category: Cabezas, E]]
+[[Category: Cabezas E]]
-[[Category: Ely, K R]]
+[[Category: Ely KR]]
-[[Category: Homma, S]]
+[[Category: Homma S]]
-[[Category: Hoyt, D W]]
+[[Category: Hoyt DW]]
-[[Category: Li, Z]]
+[[Category: Li Z]]
-[[Category: Satterthwait, A C]]
+[[Category: Satterthwait AC]]
-[[Category: Takayama, S]]
+[[Category: Takayama S]]
-[[Category: Bag domain]]
-[[Category: Bag4]]
-[[Category: Chaperone]]
-[[Category: Hsp70/hsc70 co-chaperone]]
-[[Category: Silencer of death domain]]
-[[Category: Sodd]]

1m62

From Proteopedia

Current revision

Solution structure of the BAG domain from BAG4/SODD

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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