2PGH

STRUCTURE DETERMINATION OF AQUOMET PORCINE HEMOGLOBIN AT 2.8 ANGSTROM RESOLUTION

「1PGH」から置き換えられました

2PGH の概要

• エントリーDOI: 10.2210/pdb2pgh/pdb
• 分子名称: HEMOGLOBIN (AQUO MET) (ALPHA CHAIN), HEMOGLOBIN (AQUO MET) (BETA CHAIN), PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total)
• 機能のキーワード: oxygen transport
• 由来する生物種: Sus scrofa (pig); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 64712.93

構造登録者

Katz, D.S.,White, S.P.,Huang, W.,Kumar, R.,Christianson, D.W. (登録日: 1994-09-16, 公開日: 1994-11-30, 最終更新日: 2024-02-21)

主引用文献

Katz, D.S.,White, S.P.,Huang, W.,Kumar, R.,Christianson, D.W.
Structure determination of aquomet porcine hemoglobin at 2.8 A resolution.
J.Mol.Biol., 244:541-553, 1994

PubMed Abstract: 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.

PubMed: 7990139
DOI: 10.1006/jmbi.1994.1751

実験手法

X-RAY DIFFRACTION (2.8 Å)