6II1

Crystal Structure Analysis of CO form hemoglobin from Bos taurus

6II1 の概要

• エントリーDOI: 10.2210/pdb6ii1/pdb
• 分子名称: Hemoglobin subunit alpha, Hemoglobin subunit beta, PROTOPORPHYRIN IX CONTAINING FE, ... (5 entities in total)
• 機能のキーワード: heme binding, iron ion binding, red blood cells, globin family, oxygen transport
• 由来する生物種: Bos taurus (Bovine); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 63788.00

構造登録者

Kihira, K.,Morita, Y.,Yamada, T.,Kureishi, M.,Komatsu, T. (登録日: 2018-10-03, 公開日: 2018-12-12, 最終更新日: 2023-11-22)

主引用文献

Morita, Y.,Yamada, T.,Kureishi, M.,Kihira, K.,Komatsu, T.
Quaternary Structure Analysis of a Hemoglobin Core in Hemoglobin-Albumin Cluster.
J Phys Chem B, 122:12031-12039, 2018

PubMed Abstract: A core-shell ensemble of bovine hemoglobin (Hb) and human serum albumin (HSA) is an artificial O carrier as a red blood cell substitute. This protein particle is created by covalent wrapping of a carbonyl Hb with HSAs: Hb-HSA cluster, where Hb signifies the use of carbonyl Hb (relaxed (R) state conformation) as a starting material. The Hb-HSA cluster exhibits high O affinity and low cooperativity. Analysis of the quaternary structure of the central Hb in the cluster revealed that its high O affinity is attributed to the physically immobile Hb nucleus. Circular dichroism and UV-vis absorption spectroscopy showed that the structure of deoxy Hb core closely resembles the R-state. The crystal structure of Lys-modified carbonyl Hb was superimposed on that of carbonyl Hb. These results imply that chemical modifications of the surface Lys groups and Cys-93(β) of the carbonyl Hb with cross-linking agent interfered in the quaternary structure movement from the R-state to tense (T) state. As expected, coupling of deoxy Hb (T-state) with HSAs yielded Hb-HSA cluster having low O affinity. The mixing of Hb-HSA and Hb-HSA clusters conferred a tailor-made formulation of artificial O carrier with a desired O affinity ( P).

PubMed: 30444368
DOI: 10.1021/acs.jpcb.8b10077

実験手法

X-RAY DIFFRACTION (1.34 Å)