1C7C

DEOXY RHB1.1 (RECOMBINANT HEMOGLOBIN)

1C7C の概要

• エントリーDOI: 10.2210/pdb1c7c/pdb
• 関連するPDBエントリー: 1C7B 1C7D
• 分子名称: PROTEIN (DEOXYHEMOGLOBIN (ALPHA CHAIN)), PROTEIN (DEOXYHEMOGLOBIN (BETA CHAIN)), PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total)
• 機能のキーワード: heme, oxygen delivery vehicle, blood substitute, oxygen storage-transport complex, oxygen storage/transport
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 64712.48

構造登録者

Brucker, E.A. (登録日: 2000-02-09, 公開日: 2000-06-30, 最終更新日: 2023-08-09)

主引用文献

Brucker, E.A.
Genetically crosslinked hemoglobin: a structural study.
Acta Crystallogr.,Sect.D, 56:812-816, 2000

PubMed Abstract: The crystal structures of three recombinant human hemoglobins, rHb1. 0, rHb1.1 and rHb1.2, have been determined in the deoxy state at 1.8 A resolution. Two of the three proteins, rHb1.1 and rHb1.2, contain a genetic fusion of the alpha subunits, a one- or two-glycine link, respectively, whereas rHb1.0 does not. The glycine crosslinks, localized between one N- and C--termini pair of the alpha subunits in the deoxy crystalline state, do not perturb the overall tertiary or quaternary or even the local structure of hemoglobin. Therefore, genetic fusion to prevent the dissociation of the hemoglobin tetramer, thereby inhibiting renal clearance based upon molecular size, is a structurally conservative method to stabilize hemoglobin for use as an oxygen-delivery therapeutic.

PubMed: 10930828
DOI: 10.1107/S0907444900006557

実験手法

X-RAY DIFFRACTION (1.8 Å)