1CH4

MODULE-SUBSTITUTED CHIMERA HEMOGLOBIN BETA-ALPHA (F133V)

1CH4 の概要

• エントリーDOI: 10.2210/pdb1ch4/pdb
• 分子名称: MODULE-SUBSTITUTED CHIMERA HEMOGLOBIN BETA-ALPHA, PROTOPORPHYRIN IX CONTAINING FE, CARBON MONOXIDE, ... (4 entities in total)
• 機能のキーワード: oxygen transport, chimera protein, respiratory protein, heme
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 65826.90

構造登録者

Shirai, T.,Fujikake, M.,Yamane, T.,Inaba, K.,Ishimori, K.,Morishima, I. (登録日: 1998-06-11, 公開日: 1999-04-27, 最終更新日: 2024-04-03)

主引用文献

Shirai, T.,Fujikake, M.,Yamane, T.,Inaba, K.,Ishimori, K.,Morishima, I.
Crystal structure of a protein with an artificial exon-shuffling, module M4-substituted chimera hemoglobin beta alpha, at 2.5 A resolution.
J.Mol.Biol., 287:369-382, 1999

PubMed Abstract: The crystal structure of the homotetramer of a chimera beta alpha-subunit of human hemoglobin was refined at 2.5 A resolution. The chimera subunit was constructed by replacing an exon-encoded module M4 of the beta-subunit with that of the alpha-subunit, simulating an exon-shuffling event. The implanted module M4 retained the native alpha-subunit structure, while module M3 was disturbed around the site where a new type of intron was recently found. Some of the residues were found in alternative conformations that avoid steric hindrance at the subunit interface. The modules are modestly rigid in their backbone structures by using side-chains to compensate for interface incompatibility.

PubMed: 10080899
DOI: 10.1006/jmbi.1999.2603

実験手法

X-RAY DIFFRACTION (2.5 Å)