The crystal structure of the antifungal protein zeamatin, a member of the thaumatin-like, PR-5 protein family

The crystal structure of the antifungal protein zeamatin, a member of the thaumatin-like, PR-5 protein family

The crystal structure of zeamatin, and comparisons within the family, suggest most PR-5 proteins have an electrostatically polarized surface which may be responsible for antifungal activity.

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Veröffentlicht in:Nature Structural Biology 1996-01, Vol.3 (1), p.19-22
Hauptverfasser: Batalia, Michael A, Monzingo, Arthur F, Ernst, Stephen, Roberts, Walden, Robertus, Jon D
Format: Artikel
Sprache:eng
Schlagworte:
Amino Acid Sequence
Antifungal Agents - chemistry
Arabidopsis Proteins
Biochemistry
Biological Microscopy
correspondence
Crystallography, X-Ray
Life Sciences
Membrane Biology
Molecular Sequence Data
Plant Proteins - chemistry
Protein Conformation
Protein Structure
Protein Structure, Tertiary
Trypsin Inhibitors
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Zusammenfassung:The crystal structure of zeamatin, and comparisons within the family, suggest most PR-5 proteins have an electrostatically polarized surface which may be responsible for antifungal activity.
ISSN:1072-8368
2331-365X
1545-9985
DOI:10.1038/nsb0196-19