Antifungal protein
| Antifungal_prot | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 solution structure of the antifungal protein from aspergillus giganteus. evidence for disulphide configurational isomerism | |||||||||
| Identifiers | |||||||||
| 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]
References
- ↑ 1.0 1.1 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