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SP‐40,40, a protein involved in the control of the complement pathway, possesses a unique array of disulphide bridges
Author(s) -
Kirszbaum L.,
Bozas S.E.,
Walker I.D.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)80330-j
Subject(s) - cysteine , chemistry , homology (biology) , homology modeling , in vitro , stereochemistry , biochemistry , complement membrane attack complex , disulfide bond , complement (music) , complement system , amino acid , biology , genetics , enzyme , antibody , gene , complementation , phenotype
SP‐40,40 is a two‐chain serum protein which acts in vitro as a potent inhibitor of the assembly of the membrane attack complex of human complement. It contains 10 cysteine residues, the numbers and locations of which are conserved in several mammalian species. Evidence is presented that all the cysteine residues are involved in interchain (α—β) disulphide bonds. There are no free cysteine residues. The disulphide bond motif established in this study for SP‐40,40 is unique and bears no obvious homology to those complement components whose disulphide bonds have been assigned, nor is there any homology apparent between SP‐40,40 and other multi‐chain proteins containing disulphide bonds.