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NMR solution structure of Pisum sativum defensin 2 (Psd2) provides evidence for the presence of hydrophobic surface clustersNMR solution structure of Pisum sativum defensin 2 (Psd2) provides evidence for the presence of hydrophobic surface clusters
Structural highlights
FunctionDEF2_PEA Possesses antifungal activity sensitive to inorganic cations. Publication Abstract from PubMedPisum sativum defensin 2 (Psd2) is a small (4.7 kDa) antifungal peptide whose structure is held together by four conserved disulfide bridges. Psd2 shares the cysteine-stabilized alpha-beta (CSalphabeta) 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 beta1 and alpha-helix and beta2 and beta3 sheets. The observation of surface hydrophobic clusters reveals a remarkable evolution of the CSalphabeta fold to expose and reorganize hydrophobic residues, which facilitates creating versatile binding sites. Nuclear magnetic resonance solution structure of Pisum sativum defensin 2 provides evidence for the presence of hydrophobic surface-clusters.,Pinheiro-Aguiar R, do Amaral VSG, Pereira IB, Kurtenbach E, Almeida FCL Proteins. 2019 Jul 11. doi: 10.1002/prot.25783. PMID:31294889[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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