Deamidation in proteins: The crystal structure of bovine pancreatic ribonuclease with an isoaspartyl residue at position 67

Journal of Molecular Biology

Volumn 257, Issue 3, 1996, Pages 492-496

  Capasso, S ^a   Di Donato, A ^a   Esposito, L ^a   Sica, F ^a   Sorrentino, G ^a   Vitagliano, L ^a   Zagari, A ^a   Mazzarella, L ^a  

^a UNIVERSITY OF NAPLES FEDERICO II   (Italy)

Author keywords

Crystal structure; Deamidation; Isoaspartyl residue; Ribonuclease A

Indexed keywords

ASPARAGINE; ASPARTIC ACID; PANCREATIC RIBONUCLEASE;

AMINO ACID SUBSTITUTION; ARTICLE; CATTLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; DEAMINATION; HYDROGEN BOND; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN STRUCTURE;

BOS TAURUS; BOVINAE;

EID: 0029873195     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0179     Document Type: Editorial

References (26)

1. Artigues, A., Farrant, H. & Schirch, V. (1993). Cytosolic serine hydroxymethyltransferase. Deamidation of asparaginyl residues and degradation in Xenopus laevis oocytes. J. Biol. Chem. 268, 13784-13790.
2. Bischoff, R., Lepage, P., Jaquinod, M., Cauet, G., Acker-Klein, M., Clesse, D., Laporte, M., Bayol, A., Van Dorsselaer, A. & Roitsch, C. (1993). Sequencespecific deamidation: isolation and biochemical characterization of succinimide intermediates of recombinant hirudin. Biochemistry, 32, 725-734.
3. Brennan, T. V. & Clarke, S. (1993). Spontaneous degradation of polypeptides at aspartyl and asparaginyl residues: effect of the solvent dielectric. Protein Sci. 2, 331-338.
4. Brünger, A. T. (1992). X-PLOR v3.1 User's Guide. A System for X-ray Crystallography and NMR. Yale University New Haven.
5. Capasso, S., Mazzarella, L., Sica, F. & Zagari, A. (1989). Deamidation via cyclic imide in asparaginyl peptides. Pept. Res. 2, 195-200.
6. Capasso, S., Mazzarella, L. & Zagari, A. (1991). Deamidation via cyclic imide of asparaginyl peptides: dependence on salts, buffers and organic solvents. Pept. Res. 4, 234-238.
7. Capasso, S., Kirby, A. J., Salvadori, S., Sica, F. & Zagari, A. (1995). Kinetics and mechanism of the reversible isomerization of aspartic acid residues in tetrapeptides. J. Chem. Soc. Perkin Trans. 2, 437-442.
8. Di Donato, A., Galletti, P. & D'Alessio, G. (1986). Selective deamidation and enzymatic methylation of seminal ribonuclease. Biochemistry, 25, 8361-8368.
9. Di Donato, A., Ciardiello, M. A., de Nigris, M., Piccoli, R., Mazzarella, L. & D'Alessio, G. (1993). Selective deamidation of ribonuclease A. Isolation and characterization of the resulting isoaspartyl and aspartyl derivatives. J. Biol. Chem. 268, 4745-4751.
10. Engh, R. A. & Huber, R. (1991). Accurate bond and angle parameters of X-ray protein structure refinement. Acta Crystallog. sect. A, 47, 392-400.
11. Friedman, A. R., Ichhpurani, A. K., Brown, D. M., Hillman, R. M., Krabill, L. F., Martin, R. A., Zurcher-Neely H. A. & Guido, D. M. (1991). Degradation of growth hormone releasing factor analogs in neutral aqueous solution is related to deamidation of asparagine residues. Int. J. Pept. Protein Res. 37, 14-21.
12. Geiger, T. & Clarke, S. (1987). Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides: Succinimide-linked reactions that contribute to protein degradation. J. Biol. Chem. 262, 785-794.
13. Hendrickson, W. A. (1985). Stereochemically restrained refinement of macromolecular structures. Methods Enzymol. 115, 252-270.
14. Jones, T. A. (1978). A graphics model building and refinement system for macromolecules. J. Appl. Crystallog. 11, 268-272.
15. Kossiakoff, A. A. (1988). Tertiary structure is a principal determinant to protein deamidation. Science, 240, 191-194.
16. Kraulis, P. J. (1991). MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24, 946-950.
17. Laskowski, R. A., McArthur, M. W., Moss, D. S. & Thorton, J. M. (1993). PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26, 282-291.
18. Luzzati, V. (1952). Traitement statistique des erreurs dans la determination des structures cristalline. Acta Crystallog. 5, 802-810.
19. Matthews, B. W. (1968). Solvent content of protein crystals. J. Mol. Biol. 33, 491-497.
20. Meinwald, Y. C., Stimson, E. R. & Scheraga, H. A. (1986). Deamidation of the asparaginyl-glycyl sequence. Int. J. Pept. Protein Res. 28, 79-84.
21. Montelione, G. T. & Scheraga, H. A. (1989). Formation of local structures in protein folding. Acc. Chem. Res. 22, 70-76.
22. Patel, K. & Borchardt, R. T. (1990a). Chemical pathways of peptide degradation. II. Kinetics of deamidation of an asparaginyl residue in model hexapeptide. Pharm. Res. 7, 703-711.
23. Patel, K. & Borchardt, R. T. (1990b). Chemical pathways of peptide degradation. III. Effect of primary sequence on the pathways of deamidation of asparaginyl residues in hexapeptides. Pharm. Res. 7, 787-793.
24. Tyler-Cross, R. & Schirch, V. (1991). Effects of amino acid sequence, buffers, and ionic strength on the rate and mechanism of deamidation of asparagine residues in small peptides. J. Biol. Chem. 266, 22549-22556.
25. Wlodawer, A. & Sjölin, L. (1983). Structure of ribonuclease A: results of joint neutron and X-ray refinement at 2.0 A° resolution. Biochemistry, 22, 2720-2728.
26. Wright, H. T. (1991). Non-enzymatic deamidation of asparaginyl and glutaminyl residues in proteins. Crit. Rev. Biochem. Mol. Biol. 26, 1-52.