Interaction of the chaperone calreticulin with proteins and peptides of different structural classes

Protein and Peptide Letters

Volumn 16, Issue 11, 2009, Pages 1414-1423

  Duus, K ^a   Sandhu, N ^a   Jorgensen C S ^a   Hansen, P R ^b   Steino A ^a   Thaysen Andersen, M ^c   Hojrup P ^c   Houen, G ^a  

^a STATENS SERUM INSTITUT   (Denmark)

^b UNIVERSITY OF COPENHAGEN   (Denmark)

^c UNIVERSITY OF SOUTHERN DENMARK   (Denmark)

Author keywords

Calreticulin; Chaperone; Helix, ; Peptide specificity; Sheet; Structural class,

Indexed keywords

CALRETICULIN; HEMOGLOBIN; IMMUNOGLOBULIN G; LYSOZYME; OVALBUMIN; PEPTIDE; PLACENTA PROTEIN; PROTEIN; SERUM ALBUMIN;

ARTICLE; CHEMISTRY; HUMAN; METABOLISM; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; TEMPERATURE;

CALRETICULIN; HEMOGLOBINS; HUMANS; IMMUNOGLOBULIN G; MURAMIDASE; OVALBUMIN; PEPTIDES; PREGNANCY PROTEINS; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN INTERACTION DOMAINS AND MOTIFS; PROTEIN STRUCTURE, SECONDARY; PROTEINS; SERUM ALBUMIN; TEMPERATURE;

EID: 70349937881     PISSN: 09298665     EISSN: None     Source Type: Journal    
DOI: 10.2174/092986609789353772     Document Type: Article

References (36)

1. Dobson, C.M. folding and misfolding. Nature, 2003, 426(6968), 884-890.
2. Young, J.C.; Agashe, V. R.; Siegers, K.; Hartl, F. U. Pathways of chaperone-mediated protein folding in the cytosol. Nat. Rev. Mol. Cell Biol., 2004, 5(10), 781-791.
3. Jaenicke, R. Folding and association of proteins. Prog. Biophys. Mol. Biol., 1987, 49(2-3), 117-237.
4. Levitt, M.; Chothia, C. Structural patterns in globular proteins. Nature, 1976, 261(5561), 552-558.
5. Chothia, C.; Finkelstein, A. V. The classification and origins of protein folding patterns. Annu. Rev. Biochem., 1990, 59, 1007-1039.
6. Tanford, C. Protein denaturation, Adv. Protein Chem., 1968, 23, 121-282.
7. Pace, C.N. Conformational stability of globular proteins. Trends Biochem. Sci, 1990, 15(1), 14-17.
8. Volkin, D.B.; Klibanov, A. M Minimizing protein inactivation, In Protein Function: A. Practical Approach. Creighton, T.E. Ed.; IRL Press: Oxford, 1989; pp. 1-24.
9. Wang, C.C. Protein disulfide isomerase assists protein folding as both an. isomerase and a chaperone. Ann. N. Y. Acad. Sci, 1998, 864, 9-13. (Pubitemid 29048091)
10. Schiene-Fischer, C.; Yu, C. Receptor accessory folding helper enzymes: the functional role of peptidyl prolyl cis/trans isomerases. FEBS Lett., 2001, 495(1-2), 1-6. (Pubitemid 32367963)
11. Stirling, P.C.; Bakhoum, S. F.; Feigl, A. B.; Leroux, M. R. Convergent evolution of clamp-like binding sites in diverse chaperones. Nat. Struct. Mol. Biol., 2006, 13(10), 865-870.
12. Horovitz, A.; Willison, K. R. Allosteric regulation of chaperonins. Curr. Opin. Struct. Biol., 2005, 15(6), 646-651.
13. Haslbeck, M.; Franzmann, T.; Weinfurtner, D.; Buchner, J. Some like it hot: the structure and function of small heat-shock proteins. Nat Struct. Mol. Biol., 2005, 12(10), 842-846. (Pubitemid 41486706)
14. Ni, M.; Lee, A. S. ER chaperones in mammalian development and human diseases. FEBS Lett, 2007, 581(19), 3641-3651. (Pubitemid 47082516)
15. Ellgaard, L.; Frickel, E. M. Calnexin, calreticulin, and ERp57: teammates in glycoprotein, folding. Cell Biochem. Biophys., 2003, 39(3), 223-247.
16. Williams, D.B. Beyond lectins: the calnexin/calreticulin chaperone system of the endoplasmic reticulum. J. Cell Sci, 2006, 119(4), 615-623.
17. Helenius, A.; Aebi, M. Roles of N-linked glycans in the endoplasmic reticulum. Annu. Rev. Biochem., 2004, 73, 1019-1049. (Pubitemid 39050393)
18. Sandhu, N.; Duus, K.; Jorgensen, C. S.; Hansen, P. R.; Bruun, S. W.; Pedersen, L. O.; Hojrup, P.; Houen, G. Peptide binding specificity of the chaperone calreticulin, Biochim. Biophys. Acta, 2007, 1774(6), 701-713. (Pubitemid 46863415)
19. Atherton, E.; Sheppard, R. C. Solid phase peptide synthesis. A practical approach, IRL Press: Oxford, 1989.
20. Kussmann, M.; Lassing, U.; Sturmer, C. A.; Przybylski, M.; Roepstorff, P. Matrix-assisted laser desorption/ionization mass spectrometric peptide mapping of the neural cell adhesion protein neurolin purified by sodium dodecyl sulfate Polyacrylamide gel electrophoresis or acidic precipitation. J. Mass Spectrom., 1997, 32(5), 483493. (Pubitemid 27208493)
21. Rypniewski, W.R.; Holden, H. M.; Rayment, I. Structural consequences of reductive methylation of lysine residues in. hen. egg white lysozyme: an X-ray analysis at 1.8-A resolution, Biochemistry, 1993, 32(37), 9851-9858. (Pubitemid 23296833)
22. Stein, P.E.; Leslie, A. G.; Finch, J. T.; Turnell, W. G.; McLaughlin, P. J.; Carrell, R. W. Crystal structure of ovalbumin as a model for the reactive centre of serpins. Nature, 1990, 347(6288), 99-102. (Pubitemid 20280190)
23. Stein, P.E.; Leslie, A. G.; Finch, J. T.; Carrell, R. W. Crystal structure of uncleaved ovalbumin at 1.95 A resolution. J. Mol. Biol., 1991, 221(3), 941-959. (Pubitemid 121003429)
24. Wilson, K.P.; Malcolm, B. A.; Matthews, B. W. Structural and thermodynamic analysis of compensating mutations within the core of chicken egg white lysozyme. J Biol. Chem., 1992, 267(15), 10842-10849.
25. Baldwin, J.M. The structure of human carbonmonoxy haemoglobin at 2.7 A resolution,J. Mol. Biol., 1980, 136(2), 103-128.
26. Carter, D.C.; He, X. M. Structure of human, serum albumin. Science, 1990, 249(4966), 302-303.
27. Bork, P.; Holm, L.; Sander, C. The immunoglobulin fold. Structural classification, sequence patterns and common core. J. Mol. Biol., 1994, 242(4), 309-320. (Pubitemid 2134840)
28. Amzel, L.M.; Poljak, R. J. Three-dimensional structure of immunoglobulins. Annu. Rev. Biochem., 1979, 48, 961-997.
29. Jorgensen, C.S.; Heegaard, N. H.; Holm, A.; Hojrup, P.; Houen, G. Polypeptide binding properties of the chaperone calreticulin. Eur. J Biochem., 2000, 267(10), 2945-2954. (Pubitemid 30321341)
30. Cho, J.H.; Homma, K.; Kanegasaki, S.; Natori, S. Activation of human neutrophils by a synthetic anti-microbial peptide, KLKLLLLLKLK-NH2, via cell surface calreticulin. Eur. J Biochem., 1999, 266(3), 878-885. (Pubitemid 30010105)
31. Ihara, Y.; Cohen-Doyle, M. F.; Saito, Y.; Williams, D. B. Calnexin discriminates between protein conformational states and functions as a molecular chaperone in vitro. Mol. Cell, 1999, 4(3), 331-341.
32. Danilczyk, U.G.; Williams, D. B. The lectin chaperone calnexin utilizes polypeptide-based interactions to associate with many of its substrates in vivo. J Biol. Chem., 2001, 276(27), 25532-25540. (Pubitemid 37413043)
33. Mohrluder, J.; Stangler, T.; Hoffmann, Y.; Wiesehan, K.; Mataruga, A.; Willbold, D. Identification of calreticulin as a ligand of GABARAP by phage display screening of a peptide library. FEBS J 2001, 274(21), 5543-5555.
34. Horibe, T.; Matsui, H.; Tanaka, M.; Nagai, H.; Yamaguchi, Y.; Kato, K.; Kikuchi, M. Gentamicin binds to the lectin site of calreticulin and inhibits its chaperone activity. Biochem. Biophys. Res. Commun., 2004, 323(1), 281-287. (Pubitemid 39206287)
35. Rizvi, S.M.; Mancino, L.; Thammavongsa, V.; Cantley, R. L.; Raghavan, M. A polypeptide binding conformation, of calreticulin is induced by heat shock, calcium depletion, or by deletion of the C-terminal acidic region. Mol. Cell, 2004, 15(6), 913-923. (Pubitemid 39277988)
36. Ireland, B.S.; Brockmeier, U.; Howe, C. M.; Elliott, T.; Williams, D. B. Lectin-deficient calreticulin retains full functionality as a chaperone for class I histocompatibility molecules. Mol. Biol. Cell, 2008, 19(6), 2413-2423.