Nuclear magnetic resonance solution structure of Pisum sativum Pisum sativum defensin 2 provides evidence for the presence of hydrophobic surface‐clusters

摘要

Abstract Pisum sativum defensin 2 ( Ps d2) is a small (4.7 kDa) antifungal peptide whose structure is held together by four conserved disulfide bridges. Ps d2 shares the cysteine‐stabilized alpha‐beta (CSαβ) fold, which lacks a regular hydrophobic core. All hydrophobic residues are exposed to the surface, except for leucine 6. They are clustered in the surface formed by two loops, between β1 and α‐helix and β2 and β3 sheets. The observation of surface hydrophobic clusters reveals a remarkable evolution of the CSαβ fold to expose and reorganize hydrophobic residues, which facilitates creating versatile binding sites.