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  • Title: The crystal structure of a high oxygen affinity species of haemoglobin (bar-headed goose haemoglobin in the oxy form).
    Author: Zhang J, Hua Z, Tame JR, Lu G, Zhang R, Gu X.
    Journal: J Mol Biol; 1996 Jan 26; 255(3):484-93. PubMed ID: 8568892.
    Abstract:
    We have determined the crystal structure of bar-headed goose haemoglobin in the oxy form to a resolution of 2.0 A. The R-factor of the model is 19.8%. The structure is similar to human HbA, but contacts between the subunits show slightly altered packing of the tetramer. Bar-headed goose blood shows a greatly elevated oxygen affinity compared to closely related species of geese. This is apparently due to a single proline to alanine mutation at the alpha 1 beta 1 interface which destabilises the T state of the protein. The beta chain N and C termini are well-localized, and together with other neighbouring basic groups they form a strongly positively charged groove at the entrance to the central cavity around the molecular dyad. The well-ordered conformation and the three-dimensional distribution of positive charges clearly indicate this area to be the inositol pentaphosphate binding site of bird haemoglobins.
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