Relationship between the gene and protein structure in human complement component C9
Human complement component C9 is a multidomain protein for which a large number of surface topographical features have been determined. The authors have analyzed the exon-intron boundaries of the human C9 gene and find a good correlation between splice sites and surface feature of the protein but little correlation with a putative protein domain structure, even in the cysteine-rich sequence homology with the low-density lipoprotein (LDL) receptor which is likely to be an independently folded structural motif. This is surprising because in the LDL receptor the same sequence is precisely bounded by introns, and it has been assumed that this sequence is present in both proteins as a result of exon shuffling. They deduce that substantial rearrangement of the exon-intron structure of the C9 gene must have occurred before the exchange of cysteine-rich domains, possibly linked to the process of exon duplication which was required to generate the repeats in the LDL receptor.
- Research Organization:
- European Molecular Biology Lab., Heidelberg (Germany, F.R.)
- OSTI ID:
- 6326349
- Journal Information:
- Biochemistry; (United States), Vol. 27:17
- Country of Publication:
- United States
- Language:
- English
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COMPLEMENT
AMINO ACID SEQUENCE
GENES
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GENETIC MAPPING
LIPOPROTEINS
MAN
RECOMBINANT DNA
ANIMALS
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MAMMALS
MAPPING
MOLECULAR STRUCTURE
NUCLEIC ACIDS
ORGANIC COMPOUNDS
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PROTEINS
STRUCTURAL CHEMICAL ANALYSIS
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550201* - Biochemistry- Tracer Techniques