2pgh
From Proteopedia
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STRUCTURE DETERMINATION OF AQUOMET PORCINE HEMOGLOBIN AT 2.8 ANGSTROM RESOLUTION
Overview
Considerable attention is currently focused on hemoglobins from lower, mammals, such as the pig, for potential use in cell-free blood substitute, preparations safe for use in humans. As the first step in the elucidation, of structure-function relationships in porcine hemoglobin, we have, determined the three-dimensional structure of aquomet porcine hemoglobin, at 2.8 A resolution. Overall, the porcine hemoglobin tetramer is, structurally similar to that of human oxyhemoglobin, and the r.m.s., deviation of all backbone atoms (minus five residues at the amino and, carboxyl termini of each subunit) is 0.8 A. This similarity is not, unexpected given that human and porcine hemoglobins exhibit 85% sequence, identity. However, regions of subtle structural differences are implicated, in subtle functional differences between the two proteins, such as the 20, to 25% inhibition of the alkaline Bohr effect and the accompanying, reduction in oxygen-linked chloride binding observed for porcine, hemoglobin. The structural similarity of these two mammalian hemoglobins, also rationalizes the novel hybridization behavior of pig and human, subunits in transgenic pigs expressing both porcine and human hemoglobins, in porcine erythrocytes.
About this Structure
2PGH is a Protein complex structure of sequences from Sus scrofa with HEM as ligand. This structure superseeds the now removed PDB entry 1PGH. Full crystallographic information is available from OCA.
Reference
Structure determination of aquomet porcine hemoglobin at 2.8 A resolution., Katz DS, White SP, Huang W, Kumar R, Christianson DW, J Mol Biol. 1994 Dec 16;244(5):541-53. PMID:7990139
Page seeded by OCA on Thu Nov 8 13:34:05 2007
