Antifungal protein
From Infogalactic: the planetary knowledge core
| Antifungal_prot | |||||||||
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| File:PDB 1afp EBI.jpg
solution structure of the antifungal protein from aspergillus giganteus. evidence for disulphide configurational isomerism
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| Identifiers | |||||||||
| Symbol | Antifungal_prot | ||||||||
| Pfam | PF11402 | ||||||||
| InterPro | IPR022706 | ||||||||
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In molecular biology, proteins in the antifungal protein family consist of five antiparallel beta strands which are highly twisted creating a beta barrel stabilised by four internal disulphide bridges.[1] A cationic site adjacent to a hydrophobic stretch on the protein surface may constitute a phospholipid binding site.[1]
Human epithelia produce antifungal proteins.[2] The proteins kill fungi by inducing apoptosis and/or forming pores on the cell membrane.[3]
References
This article incorporates text from the public domain Pfam and InterPro IPR022706
