Relationships between the gene and protein structure in human complement component C9.
Relationships between the gene and protein structure in human complement component C9.
复制标题
人补体成分C9基因与蛋白质结构的关系。
DOI:
10.1021/bi00417a050
复制
发表时间:
1988
期刊:
影响因子:
2.9
通讯作者:
Stanley,KK
中科院分区:
文献类型:
--
作者:
Marazziti,D;Eggertsen,G;Fey,GH;Stanley,KK
Revised Manuscript Received May 2, 1988 abstract: Human complement componentC9 is a multidomain protein for which a large number of surface topographical features have been determined. We have analyzed the exon-intron boundaries of the human C9 gene and find a good correlation betweensplice sites and surface features of the proteinbut little correlation with the 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. Wededuce that substantial rearrangement of the exon-intron structure of the C9 gene must haveoccurred 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.(Complement component C9 is an interesting protein in which to test the possible relationships between exon-intron boundaries and protein structure. Although it has notyet been crystallized, a wealth of structural features has been deter-mined by biochemical (Biesecker et al., 1982) and recombinant DNA experiments (Stanley et al., 1982; Stanley & Herz,