The high resolution crystal structure of deoxyhemoglobin S

Journal of Molecular Biology

Volumn 272, Issue 3, 1997, Pages 398-407

  Harrington, Daniel J ^a   Adachi, Kazuhikos ^b   Royer Jr , William E ^a  

^a UNIVERSITY OF MASSACHUSETTS MEDICAL SCHOOL   (United States)

^b UNIVERSITY OF PENNSYLVANIA   (United States)

Author keywords

Hemoglobin S; Molecular disease; Protein polymerization; Protein structure; Sickle cell disease

Indexed keywords

AMINO ACID; DEOXYHEMOGLOBIN; HEMOGLOBIN S; VALINE;

AMINO ACID SEQUENCE; ARTICLE; CRYSTAL STRUCTURE; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN INTERACTION; PROTEIN POLYMERIZATION; PROTEIN STRUCTURE; SICKLE CELL ANEMIA;

EID: 0031587292     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1253     Document Type: Article

References (31)

1. Adachi K., Asakura T. Nucleation-controlled aggregation of deoxyhemoglobin S. J. Biol. Chem. 254(16):1979;7765-7771.
2. Aronson H.-E. G., Royer W. E. Jr, Hendrickson W. A. Quantification of tertiary structural conservation despite primary sequence drift in the globin fold. Protein Sci. 3:1994;1706-1711.
3. Benesch R. E., Kwong S., Benesch R. The effects of alpha chain mutations cis and trans to the β6 mutation on the polymerization of sickle cell hemoglobin. Nature. 299:1982;231-234.
4. Brünger A. T. Free R value: a novel statistical quantity for assessing the accuracy of crystal structures. Nature. 355:1992a;471-475.
5. Brünger A. T. X-PLOR. 1992b;Yale University Press, New Haven.
6. Collaborative Computational Project No. 4. The CCP4 Suite: The SERC (UK) Collaborative Programs for Protein Crystallography distributed from Daresbury Laboratory, Warrington, WA4 4AD, UK. Acta Crystallog. sect. D. 50:1994;760-763.
7. Cretegny I., Edelstein S. J. Double strand packing in hemoglobin S fibers. J. Mol. Biol. 230:1993;733-738.
8. Dykes G. W., Crepeau R. H., Edelstein S. J. Three-dimensional reconstruction of 14-filament fibers of hemoglobin S. J. Mol. Biol. 130:1979;451-472.
9. Eaton W. A., Hofrichter J. Sickle cell hemoglobin polymerization. Advan. Protein Chem. 40:1990;263-279.
10. Edelstein S. J. Molecular topology in crystals and fibers of hemoglobin S. J. Mol. Biol. 150:1981;557-575.
11. Fermi G., Perutz M. F., Shaanan B., Fourme R. The crystal structure of human deoxyhaemoglobin at 1.74 Å resolution. J. Mol. Biol. 175:1984;159-174.
12. Ferrin T. E., Huang C. C., Jarvis L. E., Langridge R. The MIDAS display system. J. Mol. Graphics. 6:1988;13-27.
13. Fitzgerald P. M. D., Love W. E. Structure of deoxyhemoglobin C (beta six glu→lys) in two crystal forms. J. Mol. Biol. 132:1979;603-619.
14. Himanen J.-P., Schneider K., Chait B., Manning J. M. Participation and strength of interaction of lysine 95(β) in the polymerization of hemoglobin S as determined by its site-directed substitution to isoleucine. J. Biol. Chem. 270:1995;13885-13891.
15. Hobish M. K., Powers D. A. The binding of physiologically significant protons to 2,3-diphosphoglycerate. Biophys. Chem. 18:1983;407-411.
16. Ingram V. M. A specific chemical difference between the globins of normal human and sickle-cell anemia hemoglobin. Nature. 178:1956;792-794.
17. Jones T. A., Zou J.-Y., Cowan S. W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallog. sect. A. 47:1991;110-119.
18. Kraulis P. J. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallog. 24:1991;946-950.
19. Laskowski R. A., MacArthur M. W., Moss D. S., Thornon J. M. PROCHECK: a program to check the stereochemical quality of protein structures. J. Appl. Crystallog. 26:1993;283-291.
20. Luzzati P. V. Traitment stastique des erreurs dans ladetermination des structures cristalline. Acta Crystallog. 5:1952;802-810.
21. Magdoff-Fairchild B., Chiu C. C. X-ray diffraction studies of fibers and crystals of deoxygenated sickle-cell hemoglobin. Proc. Natl Acad. Sci. USA. 76:1979;223-226.
22. Nagel R. L., Johnson J., Bookchin R. M., Garel M. C., Rosa J., Schiliro G., Wajcman H., Labie D., Moo-Penn W., Castro O. β Chain contact sites in the hemoglobin S polymer. Nature. 283:1980;832-834.
23. Nicholls A., Bharadwaj R., Honig B. GRASP: a graphical representation and analysis of surface properties. Biophys. J. 64:1993;A166.
24. Otwinowski Z. Oscillation Data Reduction Program. Proceedings of the CCP4 Study Weekend: Data Collection and Processing. 1993;SERC Daresbury Laboratory, Warrington.
25. Padlan E. A., Love W. E. Refined crystal structure of deoxyhemoglobin S: I. Restrained least-squares refinement at 3.0 Å resolution. J. Biol. Chem. 260:1985a;8272-8279.
26. Padlan E. A., Love W. E. Refined crystal structure of deoxyhemoglobin S: II Molecular interactions in the crystal. J. Biol. Chem. 260:1985b;8280-8291.
27. Pauling L., Itano H. A., Singer S. J., Wells I. C. Sickle cell anemia, a molecular disease. Science. 110:1949;543-548.
28. Richard V., Dodson G. G., Mauguen Y. Human deoxyhaemoglobin-2,3-diphosphoglycerate complex: low-salt structure at 2.5 Å resolution. J. Mol. Biol. 233:1993;270-274.
29. Watowich S. J., Gross L. J., Josephs R. Analysis of the intermolecular contacts within sickle hemoglobin fibers: effect of site-specific substitutions, fiber pitch and double-strand disorder. J. Struct. Biol. 111:1993;161-179.
30. Wishner B. C., Ward K. B., Lattman E. E., Love W. E. Crystal structure of sickle-cell deoxyhemoglobin at 5 Å resolution. J. Mol. Biol. 98:1975;179-194.
31. Wishner B. C., Hanson J. C., Ringle W. M., Love W. E. Crystal structure of sickle-cell deoxy hemoglobin. Hercules J. I., Cottam G. L., Waterman M. R., Schechter A. N. Proceedings of the Symposium on Molecular and Cellular Aspects of Sickle Cell Disease. 1976;DHEW Publ. No. (NIH) 76-1003, Bethesda.