Antifungal protein

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PDB 1afp EBI.jpg
solution structure of the antifungal protein from aspergillus giganteus. evidence for disulphide configurational isomerism
Symbol Antifungal_prot
Pfam PF11402
InterPro IPR022706

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]


  1. ^ a b Campos-Olivas R, Bruix M, Santoro J, Lacadena J, Martinez del Pozo A, Gavilanes JG, Rico M (March 1995). "NMR solution structure of the antifungal protein from Aspergillus giganteus: evidence for cysteine pairing isomerism". Biochemistry 34 (9): 3009–21. doi:10.1021/bi00009a032. PMID 7893713. 

This article incorporates text from the public domain Pfam and InterPro IPR022706