HUMAN CELLULAR FIBRONECTIN - COMPARISON OF THE CARBOXYL-TERMINAL PORTION WITH RAT IDENTIFIES PRIMARY STRUCTURAL DOMAINS SEPARATED BY HYPERVARIABLE REGIONS
HUMAN CELLULAR FIBRONECTIN - COMPARISON OF THE CARBOXYL-TERMINAL PORTION WITH RAT IDENTIFIES PRIMARY STRUCTURAL DOMAINS SEPARATED BY HYPERVARIABLE REGIONS
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DOI:
10.1021/bi00332a016
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发表时间:
1985-01-01
期刊:
影响因子:
2.9
通讯作者:
CHU, ML
中科院分区:
文献类型:
--
作者:
BERNARD, MP;KOLBE, M;CHU, ML
The isolation and characterization of 4 overlapping cDNA clones coding for human cellular fibronectin which continuously cover > 3 kilobases in length. The nucleotide sequence of these cDNA was determined, thus elucidating the amino acid sequence of the C-terminal 794 residues of human fibronectin, which cover the edge of cellular-, heparin- and fibrin-binding domains of this protein. Comparisons of the nucleotide sequences and the deduced amino acid sequences with those of rat [Schwarzbauer, J.E., Tamkun, J.W., Lemischka, I.R., and Hynes, R.O. (1983)] indicate a high degree of conservation at both nucleotide and amino acid levels. Comparison with previously published data on amino acid sequences of bovine fibronectin made it possible to identify structurally important features of the protein during the evolution of human, calf and rat. The deduced human amino acid sequences contain 5 type III and 3 type I repeats of internal homologies. The interspecies conservation in amino acids is more pronounced in regions containing the internal repeats and within each functional domain. The implications of these interspecies conservation and divergence are discussed.