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Alpha-defensin dimers multimerize to form a pore complex
Stable Identifier
R-HSA-1461982
Type
Reaction [omitted]
Species
Homo sapiens
Compartment
plasma membrane
ReviewStatus
5/5
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Immune System (Homo sapiens)
Innate Immune System (Homo sapiens)
Antimicrobial peptides (Homo sapiens)
Defensins (Homo sapiens)
Alpha-defensins (Homo sapiens)
Alpha-defensin dimers multimerize to form a pore complex (Homo sapiens)
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Once adsorbed/inserted into the membrane, alpha defensins are believed to aggregate into pore forming structures. Based on vesicle leakage and dextran permeability experiments, Wimley et al. (1994) proposed a multimeric pore model consisting of 6-8 defensin dimers which come together to form a large pore with inner diameter of 2-2.5nm. More recently using solid-state NMR and artificial lipid bilayers, Zhang et al. (2010) provide evidence of a dimer pore model in which the polar top of the dimer lines an aqueous pore while the hydrophobic bottom faces the lipid chains. Regardless of the exact conformation, the resulting pores then allow the efflux of essential microbial cell components.
Literature References
PubMed ID
Title
Journal
Year
7833799
Interactions between human defensins and lipid bilayers: evidence for formation of multimeric pores
Wimley, WC
,
White, SH
,
Selsted, ME
Protein Sci
1994
Participants
Input
x 6
Alpha-defensin dimers:anionic phospholipids [plasma membrane]
(Homo sapiens)
Output
Alpha-defensin pore complex [plasma membrane]
(Homo sapiens)
Participates
as an event of
Alpha-defensins (Homo sapiens)
Orthologous Events
Alpha-defensin dimers multimerize to form a pore complex (Mus musculus)
Alpha-defensin dimers multimerize to form a pore complex (Rattus norvegicus)
Authored
Jupe, S (2011-04-28)
Reviewed
McDermott, AM (2011-11-03)
Created
Jupe, S (2011-07-27)
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