Interaction of the chaperone BiP with an antibody domain: Implications for the chaperone cycle

Journal of Molecular Biology

Volumn 318, Issue 3, 2002, Pages 611-620

  Knarr, Gerhard ^a   Kies, Ursula ^a   Bell, Stefan ^a   Mayer, Marcus ^a   Buchner, Johannes ^a  

^a TECHNICAL UNIVERSITY OF MUNICH   (Germany)

Author keywords

Antibodies; ATPase; Hsp70; Molecular chaperones; Protein folding

Indexed keywords

ANTIBODY; CHAPERONE; GLUCOSE REGULATED PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; BINDING SITE; COMPLEX FORMATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; SEQUENCE ANALYSIS;

EUKARYOTA;

EID: 0036303473     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)00166-3     Document Type: Article

References (51)

1. Immunoglobulin heavy chain binding protein
2. Assembly and secretion of heavy chains that do not associate posttranslationally with immunoglobulin heavy chain-binding protein
3. Designing CD4 immunoadhesins for AIDS therapy
4. BiP: A heat shock protein involved in immunoglobulin chain assembly
5. Coordination of immunoglobulin chain folding and immunoglobulin chain assembly is essential for the formation of functional IgG
6. Mapping the major interaction between binding protein and Ig light chains to sites within the variable domain
7. BiP and immunoglobulin light chain cooperate to control the folding of heavy chain and ensure the fidelity of immunoglobulin assembly
8. Enhanced transcription of the 78,000-dalton glucose-regulated protein (GRP78) gene and association of GRP78 with immunoglobulin light chains in a nonsecreting B-cell myeloma line (NS-1)
9. Association of transport-defective light chains with immunoglobulin heavy chain binding protein
10. Interaction of BiP with newly synthesized immunoglobulin light chain molecules: Cycles of sequential binding and release
11. Molecular chaperones involved in protein degradation in the endoplasmic reticulum: Quantitative interaction of the heat shock cognate protein BiP with partially folded immunoglobulin light chains that are degraded in the endoplasmic reticulum
12. The variable domain of nonassembled Ig light chains determines both their half-life and binding to the chaperone BiP
13. Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP
14. BiP-binding sequences in HIV gp160. Implications for the binding specificity of BiP
15. BiP binding sequences in antibodies
16. The crystal structure of the Fab fragment of the monoclonal antibody MAK33. Implications for folding and interaction with the chaperone BiP
17. Unassembled Ig heavy chains do not cycle from BiP in vivo but require light chains to trigger their release
18. Peptide binding and release by proteins implicated as catalysts of protein assembly
19. Peptide-binding specificity of the molecular chaperone BiP
20. Peptide-dependent stimulation of the ATPase activity of the molecular chaperone BiP is the result of conversion of oligomers to active monomers
21. Common and divergent peptide binding specificities of hsp70 molecular chaperones
22. Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries
23. The in vivo association of BiP with newly synthesized proteins is dependent on the rate and stability of folding and not simply on the presence of sequences that can bind to BiP
24. Characterization of the nucleotide binding properties and ATPase activity of recombinant hamster BiP purified from bacteria
25. Interaction of heavy chain binding protein (BiP/GRP78) with adenine nucleotides
26. Anti-chaperone behavior of BiP during the protein disulfide isomerase-catalyzed refolding of reduced denatured lysozyme
27. The role of the intrachain disulfide bond in the conformation and stability of the constant fragment of the immunoglobulin light chain
28. Reduction of the buried intrachain disulfide bond of the constant fragment of the immunoglobulin light chain: Global unfolding under physiological conditions
29. Tissue sulfhydryl groups
30. Folding and association of the antibody domain CH3: Prolyl isomerization preceeds dimerization
31. Dissociation of glucose-regulated protein Grp78 and Grp78-IgE Fc complexes by ATP
32. Interaction of BiP with substance P and nucleotides
33. ATP-induced protein-Hsp70 complex dissociation requires K + but not ATP hydrolysis
34. In vitro dissociation of BiP-peptide complexes requires a conformational change in BiP after ATP binding but does not require ATP hydrolysis
35. The second step of ATP binding to DnaK induces peptide release
36. Kinetics of molecular chaperone action
37. The power stroke of the DnaK/DnaJ/GrpE molecular chaperone system
38. Immunoglobulin heavy chain and binding protein complexes are dissociated in vivo by light chain addition
39. Inhibition of immunoglobulin folding and secretion by dominant negative BiP ATPase mutants
40. BiP and immunoglobulins light chain cooperate to control the folding heavy chain and ensure the fidelity of immunoglobulin assembly
41. Interconversion of three differentially modified and assembled forms of BiP
42. Substrate binding induces depolymerization of the C-terminal peptide binding domain of murine GRP78/BiP
43. Effect of nucleotide on the binding of peptides to 70-kDa heat shock protein
44. Interaction of nucleotide-free Hsc70 with clathrin and peptide and effect of ATP analogues
45. Kinetics of peptide binding to the bovine 70 kDa heat shock cognate protein, a molecular chaperone
46. Interaction of murine BiP/GRP78 with the DnaJ homologue MTJ1
47. J proteins catalytically activate Hsp70 molecules to trap a wide range of peptide sequences
48. Interaction of BiP with the J-domain of the Sec63p component of the endoplasmic reticulum protein translocation complex
49. A Scj1p homolog and folding catalysts present in dog pancreas microsomes
50. Homologs of the yeast Sec complex subunits Sec62p and Sec63p are abundant proteins in dog pancreas microsomes
51. cDNA cloning of the immunoglobulin heavy chain binding protein