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1hx1

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Revision as of 08:04, 18 December 2019

CRYSTAL STRUCTURE OF A BAG DOMAIN IN COMPLEX WITH THE HSC70 ATPASE DOMAIN

Structural highlights

1hx1 is a 2 chain structure with sequence from Bovin and Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	HSPA8, HSC70 (BOVIN), BAG1, HAP (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[HSP7C_BOVIN] Acts as a repressor of transcriptional activation. Inhibits the transcriptional coactivator activity of CITED1 on Smad-mediated transcription. Chaperone. Component of the PRP19-CDC5L complex that forms an integral part of the spliceosome and is required for activating pre-mRNA splicing. May have a scaffolding role in the spliceosome assembly as it contacts all other components of the core complex (By similarity). [BAG1_HUMAN] 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.^[1] ^[2] ^[3]

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 (Bcl2-associated athanogene) domains occur in a class of cofactors of the eukaryotic chaperone 70-kilodalton heat shock protein (Hsp70) family. Binding of the Bag domain to the Hsp70 adenosine triphosphatase (ATPase) domain promotes adenosine 5'-triphosphate-dependent release of substrate from Hsp70 in vitro. In a 1.9 angstrom crystal structure of a complex with the ATPase of the 70-kilodalton heat shock cognate protein (Hsc70), the Bag domain forms a three-helix bundle, inducing a conformational switch in the ATPase that is incompatible with nucleotide binding. The same switch is observed in the bacterial Hsp70 homolog DnaK upon binding of the structurally unrelated nucleotide exchange factor GrpE. Thus, functional convergence has allowed proteins with different architectures to trigger a conserved conformational shift in Hsp70 that leads to nucleotide exchange.

Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors.,Sondermann H, Scheufler C, Schneider C, Hohfeld J, Hartl FU, Moarefi I Science. 2001 Feb 23;291(5508):1553-7. PMID:11222862^[4]

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

References

↑ Takayama S, Bimston DN, Matsuzawa S, Freeman BC, Aime-Sempe C, Xie Z, Morimoto RI, Reed JC. BAG-1 modulates the chaperone activity of Hsp70/Hsc70. EMBO J. 1997 Aug 15;16(16):4887-96. PMID:9305631 doi:http://dx.doi.org/10.1093/emboj/16.16.4887
↑ Takayama S, Xie Z, Reed JC. An evolutionarily conserved family of Hsp70/Hsc70 molecular chaperone regulators. J Biol Chem. 1999 Jan 8;274(2):781-6. PMID:9873016
↑ Hung WJ, Roberson RS, Taft J, Wu DY. Human BAG-1 proteins bind to the cellular stress response protein GADD34 and interfere with GADD34 functions. Mol Cell Biol. 2003 May;23(10):3477-86. PMID:12724406
↑ Sondermann H, Scheufler C, Schneider C, Hohfeld J, Hartl FU, Moarefi I. Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors. Science. 2001 Feb 23;291(5508):1553-7. PMID:11222862 doi:10.1126/science.291.5508.1553

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/1hx1"

@@ Line 1: / Line 1: @@
 ==CRYSTAL STRUCTURE OF A BAG DOMAIN IN COMPLEX WITH THE HSC70 ATPASE DOMAIN==
-<StructureSection load='1hx1' size='340' side='right' caption='[[1hx1]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+<StructureSection load='1hx1' size='340' side='right'caption='[[1hx1]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1hx1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin] and [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HX1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1HX1 FirstGlance]. <br>
@@ Line 31: / Line 31: @@
 ==See Also==
-*[[BAG protein|BAG protein]]
+*[[BAG family proteins 3D structures|BAG family proteins 3D structures]]
+*[[Heat Shock Protein structures|Heat Shock Protein structures]]
 == References ==
 <references/>
@@ Line 38: / Line 39: @@
 [[Category: Bovin]]
 [[Category: Human]]
+[[Category: Large Structures]]
 [[Category: Moarefi, I]]
 [[Category: Scheufler, C]]

1hx1

From Proteopedia

Revision as of 08:04, 18 December 2019

CRYSTAL STRUCTURE OF A BAG DOMAIN IN COMPLEX WITH THE HSC70 ATPASE DOMAIN

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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