2D5X

Crystal structure of carbonmonoxy horse hemoglobin complexed with L35

2D5X の概要

• エントリーDOI: 10.2210/pdb2d5x/pdb
• 関連するPDBエントリー: 2D5Z 2D60
• 分子名称: Hemoglobin alpha subunit, Hemoglobin beta subunit, PROTOPORPHYRIN IX CONTAINING FE, ... (6 entities in total)
• 機能のキーワード: hemoglobin, l35, allosteric effector, oxygen storage-transport complex, oxygen storage/transport
• 由来する生物種: Equus caballus (horse); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 33226.00

構造登録者

Yokoyama, T.,Neya, S.,Tsuneshige, A.,Yonetani, T.,Park, S.Y.,Tame, J.R. (登録日: 2005-11-08, 公開日: 2006-03-07, 最終更新日: 2024-03-13)

主引用文献

Yokoyama, T.,Neya, S.,Tsuneshige, A.,Yonetani, T.,Park, S.Y.,Tame, J.R.
R-state haemoglobin with low oxygen affinity: crystal structures of deoxy human and carbonmonoxy horse haemoglobin bound to the effector molecule L35
J.Mol.Biol., 356:790-801, 2006

PubMed Abstract: Although detailed crystal structures of haemoglobin (Hb) provide a clear understanding of the basic allosteric mechanism of the protein, and how this in turn controls oxygen affinity, recent experiments with artificial effector molecules have shown a far greater control of oxygen binding than with natural heterotropic effectors. Contrary to the established text-book view, these non-physiological compounds are able to reduce oxygen affinity very strongly without switching the protein to the T (tense) state. In an earlier paper we showed that bezafibrate (BZF) binds to a surface pocket on the alpha subunits of R state Hb, strongly reducing the oxygen affinity of this protein conformation. Here we report the crystallisation of Hb with L35, a related compound, and show that this binds to the central cavity of both R and T state Hb. The mechanism by which L35 reduces oxygen affinity is discussed, in relation to spectroscopic studies of effector binding.

PubMed: 16403522
DOI: 10.1016/j.jmb.2005.12.018

実験手法

X-RAY DIFFRACTION (1.45 Å)