Abstract
Membrane attack by complement involves the self-assembly on membranes of five hydrophilic proteins (C5b, C6, C7, C8 and C9) to an amphiphilic tubular complex comprising approximately 20 subunits. The hydrophilic-amphiphilic transition of the precursor proteins is achieved by restricted unfolding and exposure of previously hidden hydrophobic domains. Restricted unfolding, in turn, is driven by high-affinity protein-protein interactions resulting in the formation of amphilic complexes. Circular polymerization of C9 to a tubular complex (poly C9) constitutes the molecular mechanism for transmembrane channel assembly and formation of ultrastructural membrane lesions.
| Original language | English |
|---|---|
| Pages (from-to) | 589-603 |
| Number of pages | 15 |
| Journal | Molecular Immunology |
| Volume | 21 |
| Issue number | 7 |
| DOIs | |
| State | Published - Jan 1 1984 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Molecular Biology
- Immunology
Cite this
Membrane attack by complement. / Podack, Eckhard R.; Tschopp, Jurg.
In: Molecular Immunology, Vol. 21, No. 7, 01.01.1984, p. 589-603.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Membrane attack by complement
AU - Podack, Eckhard R.
AU - Tschopp, Jurg
PY - 1984/1/1
Y1 - 1984/1/1
N2 - Membrane attack by complement involves the self-assembly on membranes of five hydrophilic proteins (C5b, C6, C7, C8 and C9) to an amphiphilic tubular complex comprising approximately 20 subunits. The hydrophilic-amphiphilic transition of the precursor proteins is achieved by restricted unfolding and exposure of previously hidden hydrophobic domains. Restricted unfolding, in turn, is driven by high-affinity protein-protein interactions resulting in the formation of amphilic complexes. Circular polymerization of C9 to a tubular complex (poly C9) constitutes the molecular mechanism for transmembrane channel assembly and formation of ultrastructural membrane lesions.
AB - Membrane attack by complement involves the self-assembly on membranes of five hydrophilic proteins (C5b, C6, C7, C8 and C9) to an amphiphilic tubular complex comprising approximately 20 subunits. The hydrophilic-amphiphilic transition of the precursor proteins is achieved by restricted unfolding and exposure of previously hidden hydrophobic domains. Restricted unfolding, in turn, is driven by high-affinity protein-protein interactions resulting in the formation of amphilic complexes. Circular polymerization of C9 to a tubular complex (poly C9) constitutes the molecular mechanism for transmembrane channel assembly and formation of ultrastructural membrane lesions.
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UR - http://www.scopus.com/inward/citedby.url?scp=0021256194&partnerID=8YFLogxK
U2 - 10.1016/0161-5890(84)90044-0
DO - 10.1016/0161-5890(84)90044-0
M3 - Article
C2 - 6379417
AN - SCOPUS:0021256194
VL - 21
SP - 589
EP - 603
JO - Molecular Immunology
JF - Molecular Immunology
SN - 0161-5890
IS - 7
ER -