6nom

NMR solution structure of Pisum sativum defensin 2 (Psd2) provides evidence for the presence of hydrophobic surface clusters

spinqualitylabelsall models 6nom Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6nom is a 1 chain structure with sequence from Pisum sativum. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Solution NMR, 20 models Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function DEF2_PEA Possesses antifungal activity sensitive to inorganic cations. Publication Abstract from PubMed Pisum 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Defensin 3D structures

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