Refined crystal structure of deoxyhemoglobin S. I. Restrained least-squares refinement at 3.0-A resolution.
The crystal structure of deoxyhemoglobin S has been refined at 3.0-A resolution using the Hendrickson-Konnert restrained least-squares method. Comparison with the structure of deoxyhemoglobin A reveals a hingelike movement of the beta-chain A helices, which are involved in molecular contacts, toward the EF corners of their respective subunits. This movement brings the amino termini of the beta-chains closer to the molecular dyad. The A helices remain alpha-helical throughout their entire lengths. No other major structural difference is found between deoxyhemoglobin A and deoxyhemoglobin S.
D019794:2,3-Diphosphoglycerate; D001665:Binding Sites; D003460:Crystallization; D004163:Diphosphoglyceric Acids / Q000378:metabolism; D006441:Hemoglobin A; D006451:Hemoglobin, Sickle; D006454:Hemoglobins; D006801:Humans; D046911:Macromolecular Substances; D008433:Mathematics; D008958:Models, Molecular
D004163:Diphosphoglyceric Acids; D006451:Hemoglobin, Sickle; D006454:Hemoglobins; D046911:Macromolecular Substances; D019794:2,3-Diphosphoglycerate; C100003:deoxyhemoglobin; D006441:Hemoglobin A