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Relationships between the gene and protein structure in human complement component C9.

D Marazziti1, G Eggertsen, G H Fey

  • 1European Molecular Biology Laboratory, Heidelberg, FRG.

Biochemistry
|August 23, 1988
PubMed
Summary
This summary is machine-generated.

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Human complement component C9 gene structure correlates with surface features, not protein domains. Gene rearrangements likely preceded domain exchange with LDL receptors.

Area of Science:

  • Genetics
  • Molecular Biology
  • Immunology

Background:

  • Human complement component C9 (C9) is a multidomain protein with known surface topography.
  • Cysteine-rich sequences in C9 show homology to the low-density lipoprotein (LDL) receptor.

Purpose of the Study:

  • To analyze the exon-intron structure of the human C9 gene.
  • To correlate gene structure with protein surface features and domain organization.
  • To investigate the evolutionary relationship between C9 and LDL receptor domains.

Main Methods:

  • Analysis of human C9 gene exon-intron boundaries.
  • Comparison of splice site locations with C9 surface topographical features.
  • Comparison of C9 gene structure with LDL receptor gene structure.

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Main Results:

  • A strong correlation was found between C9 gene splice sites and protein surface features.
  • Little correlation was observed between splice sites and putative protein domain structure.
  • The cysteine-rich domain homology with LDL receptor showed poor correlation with intron boundaries in C9, unlike in LDL receptor.

Conclusions:

  • The human C9 gene has undergone significant exon-intron structure rearrangement.
  • These rearrangements likely occurred before the exchange of cysteine-rich domains.
  • Exon duplication events, similar to those in the LDL receptor, may be involved in C9 evolution.