| 词条 | Antifungal protein |
| 释义 |
| Symbol = Antifungal_prot | Name = Antifungal_prot | image = PDB 1afp EBI.jpg | width = | caption = solution structure of the antifungal protein from aspergillus giganteus. evidence for disulphide configurational isomerism | Pfam = PF11402 | Pfam_clan = | InterPro = IPR022706 | SMART = | PROSITE = | MEROPS = | SCOP = | TCDB = | OPM family = | OPM protein = | CAZy = | CDD = }} 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 Epithelium produce antifungal proteins.[2] The proteins kill fungi by inducing apoptosis and/or forming pores on the cell membrane.[2] References1. ^1 {{cite journal |vauthors=Campos-Olivas R, Bruix M, Santoro J, Lacadena J, Martinez del Pozo A, Gavilanes JG, Rico M | title = NMR solution structure of the antifungal protein from Aspergillus giganteus: evidence for cysteine pairing isomerism | journal = Biochemistry | volume = 34 | issue = 9 | pages = 3009–21 |date=March 1995 | pmid = 7893713 | doi = 10.1021/bi00009a032| url = }} {{InterPro content|IPR022706}}2. ^1 {{Cite journal|last=Hein|first=Kyaw Zaw|last2=Takahashi|first2=Hitoshi|last3=Tsumori|first3=Toshiko|last4=Yasui|first4=Yukihiko|last5=Nanjoh|first5=Yasuko|last6=Toga|first6=Tetsuo|last7=Wu|first7=Zhihong|last8=Grötzinger|first8=Joachim|last9=Jung|first9=Sascha|date=2015-10-20|title=Disulphide-reduced psoriasin is a human apoptosis-inducing broad-spectrum fungicide|journal=Proceedings of the National Academy of Sciences of the United States of America|volume=112|issue=42|pages=13039–13044|doi=10.1073/pnas.1511197112|issn=1091-6490|pmc=4620902|pmid=26438863}} 1 : Protein families |
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