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

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)369-382
Number of pages14
JournalJournal of Molecular Biology
Volume287
Issue number2
DOIs
Publication statusPublished - 1999 Mar 26
Externally publishedYes

Keywords

  • Chimeric protein
  • Protein engineering
  • Protein evolution
  • Structural unit
  • X-ray crystallography

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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