Effects of different β73 amino acids on formation of 14-stranded fibers of Hb S versus double-stranded crystals of Hb C-Harlem

Biochemistry

Volumn 42, Issue 15, 2003, Pages 4476-4484

  Adachi, Kazuhiko ^a,d   Ding, Min ^a   Wehrli, Suzanne ^a   Reddy, Konda S ^b   Surrey, Saul ^c   Horiuchi, Kazumi ^a  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

^c THOMAS JEFFERSON UNIVERSITY   (United States)

^d CHILDREN S HOSPITAL OF PHILADELPHIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CRYSTALLIZATION; HYDROGEN BONDS; HYDROPHOBICITY; POLYMERIZATION;

DOUBLE-STRANDED CRYSTALS;

BIOCHEMISTRY;

AMINO ACID; ASPARAGINE; ASPARTIC ACID; HEMOGLOBIN BETA CHAIN; HEMOGLOBIN C; HEMOGLOBIN S; HISTIDINE; LEUCINE; THREONINE; UNCLASSIFIED DRUG; VALINE; HEMOGLOBIN C-HARLEM;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BINDING SITE; CONCENTRATION RESPONSE; CONTROLLED STUDY; CRYSTAL STRUCTURE; CRYSTALLIZATION; HEMOGLOBIN C HARLEM; HEMOGLOBIN DETERMINATION; HEMOGLOBIN SYNTHESIS; HUMAN; HUMAN CELL; HYDROGEN BOND; HYDROPHOBICITY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FUNCTION; PROTEIN POLYMERIZATION; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; PROTEIN VARIANT; SEQUENCE ANALYSIS; SOLUBILITY; CHEMISTRY; GENETICS; KINETICS; MUTATION; PHASE CONTRAST MICROSCOPY;

CRYSTALLIZATION; HEMOGLOBIN C; HEMOGLOBIN, SICKLE; HUMANS; KINETICS; MICROSCOPY, INTERFERENCE; MUTATION;

EID: 0037461365     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi026740x     Document Type: Article

References (19)

1. Eaton, W. A., and Hofrichter, J. (1990) Sickle cell hemoglobin polymerization, Adv. Protein Chem. 40, 63-279.
2. Dykes, G. W., Crepeau, R. H., and Edelstein, S. J. (1979) Three-dimensional reconstruction of the 14-filament fibers of hemoglobin S, J. Mol. Biol. 130, 451-472.
3. Padlan, E. A., and Love, W. E. (1985) Refined crystal structure of deoxyhemoglobin S. II. Molecular interactions in the crystal, J. Biol. Chem. 260, 8280-8291.
4. Harrington, D. J., Adachi, K., and Royer, W. E., Jr. (1997) The high-resolution crystal structure of deoxyhemoglobin S, J. Mol. Biol. 272, 398-407.
5. Bookchin, R. M., Nagel, R. L., and Ranney, H. (1967) Structure and properties of hemoglobin C Harlem, J. Biol. Chem. 242, 248-255.
6. Harrington, D. J., Adachi, K., and Royer, W. E., Jr. (1998) Crystal structure of deoxy-human hemoglobin β6 Glu→Trp, J. Biol. Chem. 273, 32690-32696.
7. Adachi, K., Kinney, T. R., Schwartz, E., and Asakura, T. (1980) Molecular stability and function of Hb C-Harlem, Hemoglobin 4, 1-26.
8. Adachi, K., and Asakura, T. (1980) Polymerization of deoxyhemoglobin C Harlem (β6Glu→Val, β73Asp→Asn), J. Mol. Biol. 144, 467-480.
9. Ivanova, M., Jasuja, R., Kransnosselskaia, L., Josephs, R., Wang, Z., Ding, M., Horiuchi, K., Adachi, K., and Ferrone, F. (2001) J. Mol. Biol. 314, 851-861.
10. Shen, T., Ho, N. T., Simplaceanu, V., Zou, M., Green, B. N., Tam, M. F., and Ho, C. (1993) Production of unmodified human adult hemoglobin in Escherichia coli, Proc. Natl. Acad. Sci. U.S.A. 90, 8108-8112.
11. Adachi, K., Konitzer, P., Kim, J., Welch, N., and Surrey, S. (1993) Effects of β6 aromatic amino acids on polymerization and solubility of recombinant hemoglobins made in yeast, J. Biol. Chem. 268, 21650-21658.
12. Adachi, K., and Asakura, T. (1979) Nucleation-controlled aggregation of deoxyhemoglobin S. Possible difference in the size of nuclei in different phosphate concentrations, J. Biol. Chem. 254, 7765-7771.
13. Yamaguchi, T., Pang, J., Reddy, K. S., Witkowska, H. E., Surrey, S., and Adachi, K. (1996) Expression of soluble human β-globin chains in bacteria and assembly in vitro with α-globin chains, J. Biol. Chem. 271, 26677-26683.
14. Samuel, R. E., Salmon, E. D., and Briehl, R. W. (1990) Nucleation and growth of fibers and gel formation in sickle cell hemoglobin, Nature 345, 833-835.
15. Briehl, R. W., and Guzman, A. E. (1994) Fragility and structure of hemoglobin S fibers and gels and their consequences for gelation kinetics and rheology, Blood 83, 573-579.
16. Wang, Z., Kischenko, G., Chen, Y., and Josephs, R. (2000) Polymerization of deoxy-sickle cell hemoglobin in high phosphate buffer, J. Struct. Biol. 131, 197-209.
17. Adachi, K., Kim, J., Kinney, T. R., and Asakura, T. (1987) Effect of β73 amino acid on the hydrophobicity, and the kinetics of polymerization of deoxyhemoglobin S, J. Biol. Chem. 262, 10470-10474.
18. Josephs, R., Jarosch, H. S., and Edelstein, S. J. (1976) Polymorphism of sickle cell hemoglobin fibers, J. Mol. Biol. 102, 409-426.
19. Ferrone, F. A., Hofrichter, J., and Eaton, W. A. (1985) Kinetics of sickle hemoglobin polymerization I: Studies using temperature-jump and laser photolysis techniques, J. Mol. Biol. 183, 611-631.