The activation of human complement component C5 by a fluid phase C5 convertase.
作者： R G DiScipio , C A Smith , H J Muller-Eberhard , T E Hugli
DOI: 10.1016/S0021-9258(17)44503-0
关键词: Binding site 、 Stereochemistry 、 Circular dichroism 、 C5-convertase 、 Cleavage (embryo) 、 Alpha chain 、 Peptide bond 、 Conformational change 、 Covalent bond 、 Chemistry
摘要: Complement component C5 is converted to C5a and C5b by the cobra venom factor-dependent C3/C5 convertase CVF,Bb (EC 3.4.21.47). The produces selective proteolytic cleavage of an arginyl-leucine peptide bond at positions 74-75 in alpha chain C5. Circular dichroism studies both far near UV regions provide evidence that a conformational change accompanies activation process. When activated presence complement C6, C5b,6 complex formed. However, when C6 added after has been C5b, fails form. Therefore, results transient binding site for C6. Hydrophobic sites are probably exposed upon because undergoes aggregation absence Transmission electron micrographs molecule indicate multilobal, irregular ultrastructure with estimated dimensions 104 X 140 168 A. Aggregated appearance globular particles diameter range 350-700 Although shares number features third complement, including similar partial sequence homology, devoid unusual thiol ester linkage found C3. It labile permits covalent attachment between C3 nucleophilic acceptors. In contrast, interactions or membranes remain noncovalent.
sci-hub.st 参考文章(56)
E M Press, J Gagnon, Human complement component C4. Structural studies on the fragments derived from C4b by cleavage with C3b inactivator Biochemical Journal. ,vol. 199, pp. 351- 357 ,(1981) , 10.1042/BJ1990351
R D Campbell, J Gagnon, R R Porter, Amino acid sequence around the thiol and reactive acyl groups of human complement component C4 Biochemical Journal. ,vol. 199, pp. 359- 370 ,(1981) , 10.1042/BJ1990359
Tony E. Hugli, Hans J. Müller-Eberhard, Anaphylatoxins: C3a and C5a. Advances in Immunology. ,vol. 26, pp. 1- 53 ,(1978) , 10.1016/S0065-2776(08)60228-X
R.P. Swenson, J.B. Howard, Amino acid sequence of the tryptic peptide containing the alkylamine-reactive site from human alpha 2-macroglobulin. Identification of gamma-glutamylmethylamide. Journal of Biological Chemistry. ,vol. 255, pp. 8087- 8091 ,(1980) , 10.1016/S0021-9258(19)70611-5
Stanford Moore, William H. Stein, [117] Chromatographic determination of amino acids by the use of automatic recording equipment Methods in Enzymology. ,vol. 6, pp. 819- 831 ,(1963) , 10.1016/0076-6879(63)06257-1
C.H.W. Hirs, [6] Determination of cystine as cysteic acid Methods in Enzymology. ,vol. 11, pp. 59- 62 ,(1967) , 10.1016/S0076-6879(67)11008-2
R B Sim, T M Twose, D S Paterson, E Sim, The covalent-binding reaction of complement component C3. Biochemical Journal. ,vol. 193, pp. 115- 127 ,(1981) , 10.1042/BJ1930115
K.E. Moon, J.P. Gorski, T.E. Hugli, Complete primary structure of human C4a anaphylatoxin. Journal of Biological Chemistry. ,vol. 256, pp. 8685- 8692 ,(1981) , 10.1016/S0021-9258(19)68898-8
H.N. Fernandez, T.E. Hugli, Primary structural analysis of the polypeptide portion of human C5a anaphylatoxin. Polypeptide sequence determination and assignment of the oligosaccharide attachment site in C5a. Journal of Biological Chemistry. ,vol. 253, pp. 6955- 6964 ,(1978) , 10.1016/S0021-9258(17)38013-4
Hans J. Müller-Eberhard, Agustin P. Dalmasso, Hemolytic Activity of Lipoprotein-Depleted Serum and the Effect of Certain Anions on Complement Journal of Immunology. ,vol. 97, pp. 680- 685 ,(1966)