1HGA
HIGH RESOLUTION CRYSTAL STRUCTURES AND COMPARISONS OF T STATE DEOXYHAEMOGLOBIN AND TWO LIGANDED T-STATE HAEMOGLOBINS: T(ALPHA-OXY)HAEMOGLOBIN AND T(MET)HAEMOGLOBIN
1HGA の概要
| エントリーDOI | 10.2210/pdb1hga/pdb |
| 分子名称 | HEMOGLOBIN (DEOXY) (ALPHA CHAIN), HEMOGLOBIN (DEOXY) (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 | Homo sapiens (human) 詳細 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 64547.05 |
| 構造登録者 | Liddington, R.,Derewenda, Z.,Dodson, E.,Hubbard, R.,Dodson, G. (登録日: 1991-10-31, 公開日: 1994-01-31, 最終更新日: 2024-05-22) |
| 主引用文献 | Liddington, R.,Derewenda, Z.,Dodson, E.,Hubbard, R.,Dodson, G. High resolution crystal structures and comparisons of T-state deoxyhaemoglobin and two liganded T-state haemoglobins: T(alpha-oxy)haemoglobin and T(met)haemoglobin. J.Mol.Biol., 228:551-579, 1992 Cited by PubMed Abstract: The origin of co-operativity in haemoglobin (Hb) resides in the reduced affinity of the T-state. T-state Hb crystals grown from polyethyleneglycol can be liganded without the molecule switching to the R high affinity state. X-ray analysis of T-state alpha-oxy Hb and T-state met Hb has identified the structural basis for reduced affinity. The nature of the chemical tension at the haem environment is different in the alpha and beta haems. There are small but definite structural changes associated with ligation in the T-state: these prove to be mostly in the same direction as the larger changes that occur in the T-->R transition. PubMed: 1453464DOI: 10.1016/0022-2836(92)90842-8 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.1 Å) |
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