| Antifungal_prot | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 solution structure of the antifungal protein from aspergillus giganteus. evidence for disulphide configurational isomerism | |||||||||
| Identifiers | |||||||||
| Symbol | Antifungal_prot | ||||||||
| Pfam | PF11402 | ||||||||
| InterPro | IPR022706 | ||||||||
| |||||||||
The antifungal protein family is a protein family, with members sharing a structure consisting 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]
- ^ 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.
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