Crystal structure of a protein with an artificial exon-shuffling, module M4-substituted chimera hemoglobin βα, at 2.5 Å resolution

Tsuyoshi Shirai, Masahiro Fujikake, Takashi Yamane, Kenji Inaba, Koichiro Ishimori, Isao Morishima

研究成果: Article査読

6 被引用数 (Scopus)

抄録

The crystal structure of the homotetramer of a chimera βα-subunit of human hemoglobin was refined at 2.5 Å resolution. The chimera subunit was constructed by replacing an exon-encoded module M4, of the β-subunit with that of the α-subunit, simulating an exon-shuffling event. The implanted module M4 retained the native α-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.

本文言語English
ページ(範囲)369-382
ページ数14
ジャーナルJournal of Molecular Biology
287
2
DOI
出版ステータスPublished - 1999 3月 26
外部発表はい

ASJC Scopus subject areas

  • 構造生物学
  • 分子生物学

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