General Information

    • DRAMP ID

    • DRAMP03779

    • Peptide Name

    • Antifungal protein (AFP; Fungi)

    • Source

    • Aspergillus giganteus

    • Family

    • Not found

    • Gene

    • afp

    • Sequence

    • XTYNGKCYKKDNICKYKAQSGKTAICKCYVKKCPRDGAKCEFDSYKGKCYC

    • Sequence Length

    • 51

    • Protein Existence

    • Protein level

Activity Information

    • Biological Activity

    • Antimicrobial, Antifungal

    • Target Organism

    • No MICs found in DRAMP database

    • Hemolytic Activity

      • No hemolysis information or data found in the reference(s) presented in this entry

    • Cytotoxicity

      • Not included yet

    • Binding Target

    • Phospholipids

Structure Information

    • Linear/Cyclic

    • Not included yet

    • N-terminal Modification

    • Not included yet

    • C-terminal Modification

    • Not included yet

    • Nonterminal Modifications and Unusual Amino Acids

    • Not included yet

    • Stereochemistry

    • Not included yet

    • Structure

    • Beta strand (6 strands; 15 residues)

    • Structure Description

    • The folding of AFP consists of five antiparallel beta strands connected in a -1, -1, +3, +1 topology and highly twisted, defining a small and compact beta barrel stabilized by four internal disulfide bridges. A cationic site formed by up to three lysine side chains adjacent to a hydrophobic stretch, both at the protein surface, may constitute a potential binding site for phospholipids which would be the basis of its biological function.

    • Helical Wheel Diagram

    • DRAMP03779 helical wheel diagram

    • PDB ID

    • 1AFP resolved by NMR.

    • Predicted Structure

    • There is no predicted structure for DRAMP03779.

Physicochemical Information

    • Formula

    • C248H390N68O71S8

    • Absent Amino Acids

    • HLMW

    • Common Amino Acids

    • K

    • Mass

    • 5846.06

    • PI

    • 9.27

    • Basic Residues

    • 13

    • Acidic Residues

    • 4

    • Hydrophobic Residues

    • 7

    • Net Charge

    • +9

    • Boman Index

    • -109.8

    • Hydrophobicity

    • -0.949

    • Aliphatic Index

    • 26.86

    • Half Life

      • Mammalian:?
      • Yeast:?
      • E.coli:?

    • Extinction Coefficient Cystines

    • 9440

    • Absorbance 280nm

    • 188.8

    • Polar Residues

    • 24

DRAMP03779

DRAMP03779 chydropathy plot

Comments Information

    • Function

    • This protein inhibits the growth of a variety of fungal species.

    • PTM

    • Contains four disulfide bonds 7-33; 14-40; 26-28; 49-51.

Literature Information

  • ·Literature 1

    • Title

    • Amino acid sequence and disulfide bridges of an antifungal protein isolated from Aspergillus giganteus.

    • Reference

    • Eur J Biochem. 1990 Oct 5;193(1):31-38.

    • Author

    • Nakaya K, Omata K, Okahashi I, Nakamura Y, Kolekenbrock H, Ulbrich N.
  • ·Literature 2

    • Title

    • NMR solution structure of the antifungal protein from Aspergillus giganteus: evidence for cysteine pairing isomerism.

    • Reference

    • Biochemistry. 1995 Mar 7;34(9):3009-3021.

    • Author

    • Campos-Olivas R, Bruix M, Santoro J, Lacadena J, Martinez del Pozo A, Gavilanes JG, Rico M.