Relationship between the gene and protein structure in human complement component C9

Journal Article · Tue Aug 23 04:00:00 EDT 1988 · Biochemistry; (United States)

DOI:https://doi.org/10.1021/bi00417a050· OSTI ID:6326349

Marazziti, D; Eggertsen, G; Fey, G H; Stanley, K K

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), Journal Name: Biochemistry; (United States) Vol. 27:17; ISSN BICHA
• Country of Publication: United States
• Language: English

Related Subjects

550201* -- Biochemistry-- Tracer Techniques
59 BASIC BIOLOGICAL SCIENCES
AMINO ACID SEQUENCE
ANIMALS
COMPLEMENT
DNA
DNA SEQUENCING
GENES
GENETIC MAPPING
LIPIDS
LIPOPROTEINS
MAMMALS
MAN
MAPPING
MOLECULAR STRUCTURE
NUCLEIC ACIDS
ORGANIC COMPOUNDS
PRIMATES
PROTEINS
RECOMBINANT DNA
STRUCTURAL CHEMICAL ANALYSIS
VERTEBRATES