An X-ray determination of the molecular interactions in hemoglobin C: A disease characterized by intraerythrocytic crystals
| Autor: | T.E. Houston, Titus H.J. Huisman, R. L. Girling, Elmer L. Amma |
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| Rok vydání: | 1979 |
| Předmět: |
Erythrocytes
Macromolecular Substances Protein Conformation Biophysics Biochemistry Square (algebra) law.invention X-Ray Diffraction law Position (vector) Nitriles medicine Humans Molecule Crystallization Molecular Biology Methemoglobin Molecular interactions Chemistry Hemoglobin C X-ray Cell Biology Hemoglobin C Disease medicine.disease Crystallography Hemoglobin |
| Zdroj: | Biochemical and Biophysical Research Communications. 88:768-773 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/0006-291x(79)91474-8 |
| Popis: | The X-ray structure of cyanomet human hemoglobin C has been solved and refined, R ∼27%. The molecular packing can be represented in two dimensions by two sets of parallel strands, one set in the b direction and the other in the c direction. Taken together the two sets of strands interconnect the molecules into square nets or layers where each molecule contacts its four nearest neighbors. Molecules in one layer are displaced in a and b so that they fit into the “holes” of the square arrays of the adjacent layers (normal to a ) resulting in a pseudo body-centered cubic packing. This packing can account for the hemoglobin crystallization in and fragility of the erythrocytes. The aberrant β6A3 Lys residue is in a position to influence the crystal formation. |
| Databáze: | OpenAIRE |
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