1H NMR structure of an antifungal gamma-thionin protein SIalpha1: similarity to scorpion toxins.
Proteins
; 32(3): 334-49, 1998 Aug 15.
Article
in En
| MEDLINE
| ID: mdl-9715910
ABSTRACT
The three-dimensional structure of the Sorghum bicolor seed protein gamma-thionin SIalpha1 has been determined by 2D 1H nuclear magnetic resonance (NMR) spectroscopy. The secondary structure of this 47-residue antifungal protein with four disulphide bridges consists of a three-stranded antiparallel sheet and one helix. The helix is tethered to the sheet by two disulphide bridges which link two successive turns of the helix to alternate residues i, i+2 in one strand. Possible binding sites for antifungal activity are discussed. The same fold has been observed previously in several scorpion toxins.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Plant Proteins
/
Scorpion Venoms
/
Arabidopsis Proteins
/
Antifungal Agents
Language:
En
Journal:
Proteins
Journal subject:
BIOQUIMICA
Year:
1998
Document type:
Article
Affiliation country:
United kingdom