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Chaperone/chaperone inhibitor PDB id
1hx1
Jmol
Contents
Protein chains
377 a.a. *
112 a.a. *
Ligands
TRS
Waters ×359
* Residue conservation analysis
PDB id:
1hx1
Name: Chaperone/chaperone inhibitor
Title: Crystal structure of a bag domain in complex with the hsc70 domain
Structure: Heat shock cognate 71 kda. Chain: a. Fragment: atpase domain. Synonym: hsc70. Engineered: yes. Bag-family molecular chaperone regulator-1. Chain: b. Fragment: bag domain. Synonym: bag-1.
Source: Bos taurus. Cattle. Organism_taxid: 9913. Expressed in: escherichia coli. Expression_system_taxid: 562. Homo sapiens. Human. Organism_taxid: 9606. Expression_system_taxid: 562
Biol. unit: Dimer (from PQS)
Resolution:
1.90Å     R-factor:   0.234     R-free:   0.279
Authors: H.Sondermann,C.Scheufler,I.Moarefi
Key ref:
H.Sondermann et al. (2001). Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors. Science, 291, 1553-1557. PubMed id: 11222862 DOI: 10.1126/science.1057268
Date:
11-Jan-01     Release date:   07-Mar-01    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P19120  (HSP7C_BOVIN) -  Heat shock cognate 71 kDa protein
Seq:
Struc: 		 
Seq:
Struc: 		650 a.a.
377 a.a.
Protein chain
Pfam   ArchSchema ?
Q99933  (BAG1_HUMAN) -  BAG family molecular chaperone regulator 1
Seq:
Struc: 		345 a.a.
112 a.a.*
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biochemical function     chaperone binding     2 terms  

 

 
DOI no: 10.1126/science.1057268 Science 291:1553-1557 (2001)
PubMed id: 11222862  
 
 
Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors.
H.Sondermann, C.Scheufler, C.Schneider, J.Hohfeld, F.U.Hartl, I.Moarefi.
 
  ABSTRACT  
 
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.
 
  Selected figure(s)  
 
Figure 2.
Fig. 2. The Bag domain/Hsc70 complex. (A) The backbones of the Bag domain (red) and the ATPase domain of Hsc70 (green) shown in a ribbons representation generated with the program Bobscript (38). (B) The electrostatic potential of the Bag domain/Hsc70 (residues 5-381) complex modeled onto the accessible molecular surface as calculated and visualized with GRASP (39). Red and blue indicate negative and positive charges, respectively. Orientation as in (A). (C) Schematic diagram of the interactions between Hsc70 and the Bag domain. The diagram was produced by LIGPLOT (40). Red, residues of Bag-1M; green, residues of Hsc70. (D) Structure-based sequence alignment of Bag do- main proteins from different species. Conserved residues forming the interaction surface with the Hsc70 ATPase domain are highlighted in red, and residues important for packing interactions are shown in blue (41). GenBank accession numbers are as follows: human Bag-1M human (hum), Q99933; human Bag-3/CAIR/BIS, AAD16122; human Bag-4, AAD16123; human Bag-5, AAD16124; Caenorhabditis elegans (C.e) Bag-1, AAD16125; Schizosaccharomyces pombe (S.p) Bag-1B, AAD16127; Saccharomyces cerevisiae (S.c) Snl1p, NP_012248; Arabidopsis thaliana (A.t) putative protein, CAB87278; and Drosophila melanogaster (D.m) gene product, AAF49807. 		Figure 3.
Fig. 3. Structural comparison of (A) Bag domain/Hsc70 and (B) DnaK/GrpE complexes. The ATPase domains of Hsc70 and DnaK are colored green, the Bag domain is red, and GrpE is yellow.
 
  The above figures are reprinted by permission from the AAAs: Science (2001, 291, 1553-1557) copyright 2001.  
  Figures were selected by the author.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
21482798 A.Zhuravleva, and L.M.Gierasch (2011).
Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones.
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Ubiquitinylation of α-Synuclein by Carboxyl Terminus Hsp70-Interacting Protein (CHIP) Is Regulated by Bcl-2-Associated Athanogene 5 (BAG5).
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21252941 M.Gamerdinger, A.M.Kaya, U.Wolfrum, A.M.Clement, and C.Behl (2011).
BAG3 mediates chaperone-based aggresome-targeting and selective autophagy of misfolded proteins.
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20223214 A.Arakawa, N.Handa, N.Ohsawa, M.Shida, T.Kigawa, F.Hayashi, M.Shirouzu, and S.Yokoyama (2010).
The C-terminal BAG domain of BAG5 induces conformational changes of the Hsp70 nucleotide-binding domain for ADP-ATP exchange.
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PDB codes: 1ugo 1uk5 2d9d 3a8y
20018538 A.Bhattacharya, M.Revington, and E.R.Zuiderweg (2010).
Measurement and interpretation of 15N-1H residual dipolar couplings in larger proteins.
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A novel, small molecule inhibitor of Hsc70/Hsp70 potentiates Hsp90 inhibitor induced apoptosis in HCT116 colon carcinoma cells.
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AtBAG7, an Arabidopsis Bcl-2-associated athanogene, resides in the endoplasmic reticulum and is involved in the unfolded protein response.
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20453930 J.C.Young (2010).
Mechanisms of the Hsp70 chaperone system.
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20368414 M.Ammirante, A.Rosati, C.Arra, A.Basile, A.Falco, M.Festa, M.Pascale, M.d'Avenia, L.Marzullo, M.A.Belisario, M.De Marco, A.Barbieri, A.Giudice, G.Chiappetta, E.Vuttariello, M.Monaco, P.Bonelli, G.Salvatore, M.Di Benedetto, S.L.Deshmane, K.Khalili, M.C.Turco, and A.Leone (2010).
IKK{gamma} protein is a target of BAG3 regulatory activity in human tumor growth.
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19845507 M.Fuchs, D.J.Poirier, S.J.Seguin, H.Lambert, S.Carra, S.J.Charette, and J.Landry (2010).
Identification of the key structural motifs involved in HspB8/HspB6-Bag3 interaction.
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20179333 M.Shida, A.Arakawa, R.Ishii, S.Kishishita, T.Takagi, M.Kukimoto-Niino, S.Sugano, A.Tanaka, M.Shirouzu, and S.Yokoyama (2010).
Direct inter-subdomain interactions switch between the closed and open forms of the Hsp70 nucleotide-binding domain in the nucleotide-free state.
  Acta Crystallogr D Biol Crystallogr, 66, 223-232.
PDB codes: 2e88 2e8a
20072699 M.Wisniewska, T.Karlberg, L.Lehtiö, I.Johansson, T.Kotenyova, M.Moche, and H.Schüler (2010).
Crystal structures of the ATPase domains of four human Hsp70 isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and HSPA5/BiP/GRP78.
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PDB codes: 3fe1 3gdq 3i33 3iuc 3jxu
20156966 S.Deeg, M.Gralle, K.Sroka, M.Bähr, F.S.Wouters, and P.Kermer (2010).
BAG1 restores formation of functional DJ-1 L166P dimers and DJ-1 chaperone activity.
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  19908379 Y.Liu, and I.Bahar (2010).
Toward understanding allosteric signaling mechanisms in the ATPase domain of molecular chaperones.
  Pac Symp Biocomput, 0, 269-280.  
  20862304 Y.Liu, L.M.Gierasch, and I.Bahar (2010).
Role of Hsp70 ATPase domain intrinsic dynamics and sequence evolution in enabling its functional interactions with NEFs.
  PLoS Comput Biol, 6, 0.  
19361428 A.Bhattacharya, A.V.Kurochkin, G.N.Yip, Y.Zhang, E.B.Bertelsen, and E.R.Zuiderweg (2009).
Allostery in Hsp70 chaperones is transduced by subdomain rotations.
  J Mol Biol, 388, 475-490.  
18819021 A.M.Chow, R.Steel, and R.L.Anderson (2009).
Hsp72 chaperone function is dispensable for protection against stress-induced apoptosis.
  Cell Stress Chaperones, 14, 253-263.  
19690191 A.Sharp, S.J.Crabb, P.W.Johnson, A.Hague, R.Cutress, P.A.Townsend, A.Ganesan, and G.Packham (2009).
Thioflavin S (NSC71948) interferes with Bcl-2-associated athanogene (BAG-1)-mediated protein-protein interactions.
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19519514 D.Sharma, and D.C.Masison (2009).
Hsp70 structure, function, regulation and influence on yeast prions.
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19056335 D.W.Pettigrew (2009).
Amino acid substitutions in the sugar kinase/hsp70/actin superfamily conserved ATPase core of E. coli glycerol kinase modulate allosteric ligand affinity but do not alter allosteric coupling.
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19819219 D.W.Pettigrew (2009).
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19883127 H.J.Woo, J.Jiang, E.M.Lafer, and R.Sousa (2009).
ATP-induced conformational changes in Hsp70: molecular dynamics and experimental validation of an in silico predicted conformation.
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19151744 H.Y.Liu, Z.M.Wang, Y.Bai, M.Wang, Y.Li, S.Wei, Q.H.Zhou, and J.Chen (2009).
Different BAG-1 isoforms have distinct functions in modulating chemotherapeutic-induced apoptosis in breast cancer cells.
  Acta Pharmacol Sin, 30, 235-241.  
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To fold or not to fold: modulation and consequences of Hsp90 inhibition.
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Linker histones stimulate HSPA2 ATPase activity through NASP binding and inhibit CDC2/Cyclin B1 complex formation during meiosis in the mouse.
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19860737 S.Patury, Y.Miyata, and J.E.Gestwicki (2009).
Pharmacological targeting of the Hsp70 chaperone.
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19399228 U.Gehring (2009).
Multiple, but Concerted Cellular Activities of the Human Protein Hap46/BAG-1M and Isoforms.
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The BAG-1 cochaperone is a negative regulator of p73-dependent transcription.
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18550409 J.P.Schuermann, J.Jiang, J.Cuellar, O.Llorca, L.Wang, L.E.Gimenez, S.Jin, A.B.Taylor, B.Demeler, K.A.Morano, P.J.Hart, J.M.Valpuesta, E.M.Lafer, and R.Sousa (2008).
Structure of the Hsp110:Hsc70 nucleotide exchange machine.
  Mol Cell, 31, 232-243.
PDB code: 3c7n
18555782 S.Polier, Z.Dragovic, F.U.Hartl, and A.Bracher (2008).
Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding.
  Cell, 133, 1068-1079.
PDB codes: 3d2e 3d2f
19029896 Z.Xu, R.C.Page, M.M.Gomes, E.Kohli, J.C.Nix, A.B.Herr, C.Patterson, and S.Misra (2008).
Structural basis of nucleotide exchange and client binding by the Hsp70 cochaperone Bag2.
  Nat Struct Mol Biol, 15, 1309-1317.
PDB codes: 3cqx 3d0t
17493862 A.Rosati, M.Ammirante, A.Gentilella, A.Basile, M.Festa, M.Pascale, L.Marzullo, M.A.Belisario, A.Tosco, S.Franceschelli, O.Moltedo, G.Pagliuca, R.Lerose, and M.C.Turco (2007).
Apoptosis inhibition in cancer cells: a novel molecular pathway that involves BAG3 protein.
  Int J Biochem Cell Biol, 39, 1337-1342.  
17766381 A.Shonhai, A.Boshoff, and G.L.Blatch (2007).
The structural and functional diversity of Hsp70 proteins from Plasmodium falciparum.
  Protein Sci, 16, 1803-1818.  
17475647 C.A.Kyratsous, and S.J.Silverstein (2007).
BAG3, a host cochaperone, facilitates varicella-zoster virus replication.
  J Virol, 81, 7491-7503.  
17434124 J.F.Swain, G.Dinler, R.Sivendran, D.L.Montgomery, M.Stotz, and L.M.Gierasch (2007).
Hsp70 chaperone ligands control domain association via an allosteric mechanism mediated by the interdomain linker.
  Mol Cell, 26, 27-39.  
17513460 K.A.Morano (2007).
New tricks for an old dog: the evolving world of Hsp70.
  Ann N Y Acad Sci, 1113, 1.  
17283040 K.M.Hatle, W.Neveu, O.Dienz, S.Rymarchyk, R.Barrantes, S.Hale, N.Farley, K.M.Lounsbury, J.P.Bond, D.Taatjes, and M.Rincón (2007).
Methylation-controlled J protein promotes c-Jun degradation to prevent ABCB1 transporter expression.
  Mol Cell Biol, 27, 2952-2966.  
17441502 L.Shaner, and K.A.Morano (2007).
All in the family: atypical Hsp70 chaperones are conserved modulators of Hsp70 activity.
  Cell Stress Chaperones, 12, 1-8.  
17469204 L.Xu, S.E.Sedelnikova, P.J.Baker, A.Hunt, J.Errington, and D.W.Rice (2007).
Crystal structure of S. aureus YlaN, an essential leucine rich protein involved in the control of cell shape.
  Proteins, 68, 438-445.
PDB code: 2odm
17596514 M.K.Bhangoo, S.Tzankov, A.C.Fan, K.Dejgaard, D.Y.Thomas, and J.C.Young (2007).
Multiple 40-kDa heat-shock protein chaperones function in Tom70-dependent mitochondrial import.
  Mol Biol Cell, 18, 3414-3428.  
17804463 M.Stahl, M.Retzlaff, M.Nassal, and J.Beck (2007).
Chaperone activation of the hepadnaviral reverse transcriptase for template RNA binding is established by the Hsp70 and stimulated by the Hsp90 system.
  Nucleic Acids Res, 35, 6124-6136.  
17923091 Q.Liu, and W.A.Hendrickson (2007).
Insights into Hsp70 chaperone activity from a crystal structure of the yeast Hsp110 Sse1.
  Cell, 131, 106-120.
PDB code: 2qxl
17065559 S.H.Park, N.Bolender, F.Eisele, Z.Kostova, J.Takeuchi, P.Coffino, and D.H.Wolf (2007).
The cytoplasmic Hsp70 chaperone machinery subjects misfolded and endoplasmic reticulum import-incompetent proteins to degradation via the ubiquitin-proteasome system.
  Mol Biol Cell, 18, 153-165.  
17964199 T.M.Buck, C.M.Wright, and J.L.Brodsky (2007).
The activities and function of molecular chaperones in the endoplasmic reticulum.
  Semin Cell Dev Biol, 18, 751-761.  
16678092 B.Bukau, J.Weissman, and A.Horwich (2006).
Molecular chaperones and protein quality control.
  Cell, 125, 443-451.  
16003391 C.H.Kang, W.Y.Jung, Y.H.Kang, J.Y.Kim, D.G.Kim, J.C.Jeong, D.W.Baek, J.B.Jin, J.Y.Lee, M.O.Kim, W.S.Chung, T.Mengiste, H.Koiwa, S.S.Kwak, J.D.Bahk, S.Y.Lee, J.S.Nam, D.J.Yun, and M.J.Cho (2006).
AtBAG6, a novel calmodulin-binding protein, induces programmed cell death in yeast and plants.
  Cell Death Differ, 13, 84-95.  
16688211 H.Raviol, H.Sadlish, F.Rodriguez, M.P.Mayer, and B.Bukau (2006).
Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor.
  EMBO J, 25, 2510-2518.  
16482527 M.Krajewska, B.C.Turner, A.Shabaik, S.Krajewski, and J.C.Reed (2006).
Expression of BAG-1 protein correlates with aggressive behavior of prostate cancers.
  Prostate, 66, 801-810.  
17026666 R.Sousa, and E.M.Lafer (2006).
Keep the traffic moving: mechanism of the Hsp70 motor.
  Traffic, 7, 1596-1603.  
17132105 Z.Dragovic, Y.Shomura, N.Tzvetkov, F.U.Hartl, and A.Bracher (2006).
Fes1p acts as a nucleotide exchange factor for the ribosome-associated molecular chaperone Ssb1p.
  Biol Chem, 387, 1593-1600.  
16307916 J.Jiang, K.Prasad, E.M.Lafer, and R.Sousa (2005).
Structural basis of interdomain communication in the Hsc70 chaperone.
  Mol Cell, 20, 513-524.
PDB code: 1yuw
15831476 J.Liman, S.Ganesan, C.P.Dohm, S.Krajewski, J.C.Reed, M.Bähr, F.S.Wouters, and P.Kermer (2005).
Interaction of BAG1 and Hsp70 mediates neuroprotectivity and increases chaperone activity.
  Mol Cell Biol, 25, 3715-3725.  
16143622 M.Coulson, S.Robert, and R.Saint (2005).
Drosophila starvin encodes a tissue-specific BAG-domain protein required for larval food uptake.
  Genetics, 171, 1799-1812.  
15678420 M.Groll, M.Bochtler, H.Brandstetter, T.Clausen, and R.Huber (2005).
Molecular machines for protein degradation.
  Chembiochem, 6, 222-256.  
15770419 M.P.Mayer, and B.Bukau (2005).
Hsp70 chaperones: cellular functions and molecular mechanism.
  Cell Mol Life Sci, 62, 670-684.  
15474970 P.A.Townsend, A.Stephanou, G.Packham, and D.S.Latchman (2005).
BAG-1: a multi-functional pro-survival molecule.
  Int J Biochem Cell Biol, 37, 251-259.  
16207813 V.Arndt, C.Daniel, W.Nastainczyk, S.Alberti, and J.Höhfeld (2005).
BAG-2 acts as an inhibitor of the chaperone-associated ubiquitin ligase CHIP.
  Mol Biol Cell, 16, 5891-5900.  
15937186 V.Oganesyan, N.Oganesyan, P.D.Adams, J.Jancarik, H.A.Yokota, R.Kim, and S.H.Kim (2005).
Crystal structure of the "PhoU-like" phosphate uptake regulator from Aquifex aeolicus.
  J Bacteriol, 187, 4238-4244.
PDB codes: 1t72 1t8b
15694338 Y.Shomura, Z.Dragovic, H.C.Chang, N.Tzvetkov, J.C.Young, J.L.Brodsky, V.Guerriero, F.U.Hartl, and A.Bracher (2005).
Regulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange.
  Mol Cell, 17, 367-379.
PDB codes: 1xqr 1xqs
15169918 B.M.Pickering, S.A.Mitchell, K.A.Spriggs, M.Stoneley, and A.E.Willis (2004).
Bag-1 internal ribosome entry segment activity is promoted by structural changes mediated by poly(rC) binding protein 1 and recruitment of polypyrimidine tract binding protein 1.
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15459659 J.C.Young, V.R.Agashe, K.Siegers, and F.U.Hartl (2004).
Pathways of chaperone-mediated protein folding in the cytosol.
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15342595 J.P.Suppini, M.Amor, J.H.Alix, and M.M.Ladjimi (2004).
Complementation of an Escherichia coli DnaK defect by Hsc70-DnaK chimeric proteins.
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15333932 J.Symersky, Y.Zhang, N.Schormann, S.Li, R.Bunzel, P.Pruett, C.H.Luan, and M.Luo (2004).
Structural genomics of Caenorhabditis elegans: structure of the BAG domain.
  Acta Crystallogr D Biol Crystallogr, 60, 1606-1610.
PDB code: 1t7s
14991745 M.Rusin, H.Zientek, M.Krześniak, E.Małusecka, A.Zborek, S.Krzyzowska-Gruca, D.Butkiewicz, R.Vaitiekunaite, K.Lisowska, E.Grzybowska, and Z.Krawczyk (2004).
Intronic polymorphism (1541-1542delGT) of the constitutive heat shock protein 70 gene has functional significance and shows evidence of association with lung cancer risk.
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15560850 R.Götz, B.W.Kramer, G.Camarero, and U.R.Rapp (2004).
BAG-1 haplo-insufficiency impairs lung tumorigenesis.
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Integral UBL domain proteins: a family of proteasome interacting proteins.
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15215316 S.Alberti, K.Böhse, V.Arndt, A.Schmitz, and J.Höhfeld (2004).
The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator.
  Mol Biol Cell, 15, 4003-4010.  
14704958 S.Jablonka, S.Wiese, and M.Sendtner (2004).
Axonal defects in mouse models of motoneuron disease.
  J Neurobiol, 58, 272-286.  
15603737 S.K.Kalia, S.Lee, P.D.Smith, L.Liu, S.J.Crocker, T.E.Thorarinsdottir, J.R.Glover, E.A.Fon, D.S.Park, and A.M.Lozano (2004).
BAG5 inhibits parkin and enhances dopaminergic neuron degeneration.
  Neuron, 44, 931-945.  
14755308 U.Gehring (2004).
Biological activities of HAP46/BAG-1. The HAP46/BAG-1 protein: regulator of HSP70 chaperones, DNA-binding protein and stimulator of transcription.
  EMBO Rep, 5, 148-153.  
15232009 Y.Zhang, and E.R.Zuiderweg (2004).
The 70-kDa heat shock protein chaperone nucleotide-binding domain in solution unveiled as a molecular machine that can reorient its functional subdomains.
  Proc Natl Acad Sci U S A, 101, 10272-10277.  
12853476 A.Brychzy, T.Rein, K.F.Winklhofer, F.U.Hartl, J.C.Young, and W.M.Obermann (2003).
Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system.
  EMBO J, 22, 3613-3623.  
15115283 C.Y.Fan, S.Lee, and D.M.Cyr (2003).
Mechanisms for regulation of Hsp70 function by Hsp40.
  Cell Stress Chaperones, 8, 309-316.  
14506847 C.Yost, L.Hauser, F.Larimer, D.Thompson, A.Beliaev, J.Zhou, Y.Xu, and D.Xu (2003).
A computational study of Shewanella oneidensis MR-1: structural prediction and functional inference of hypothetical proteins.
  OMICS, 7, 177-191.  
12517345 D.I.Liao, L.Reiss, I.Turner, and G.Dotson (2003).
Structure of glycerol dehydratase reactivase: a new type of molecular chaperone.
  Structure, 11, 109-119.
PDB code: 1nbw
12832480 H.H.Kampinga, B.Kanon, F.A.Salomons, A.E.Kabakov, and C.Patterson (2003).
Overexpression of the cochaperone CHIP enhances Hsp70-dependent folding activity in mammalian cells.
  Mol Cell Biol, 23, 4948-4958.  
12824481 I.Halperin, H.Wolfson, and R.Nussinov (2003).
SiteLight: binding-site prediction using phage display libraries.
  Protein Sci, 12, 1344-1359.  
14559183 J.C.Young, J.M.Barral, and F.Ulrich Hartl (2003).
More than folding: localized functions of cytosolic chaperones.
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