6NOM
NMR solution structure of Pisum sativum defensin 2 (Psd2) provides evidence for the presence of hydrophobic surface clusters
Summary for 6NOM
| Entry DOI | 10.2210/pdb6nom/pdb |
| NMR Information | BMRB: 30561 |
| Descriptor | Defensin-2 (1 entity in total) |
| Functional Keywords | psd1, psd2, plant defensins, antimicrobial peptides, antimicrobial protein |
| Biological source | Pisum sativum (Garden pea) |
| Total number of polymer chains | 1 |
| Total formula weight | 5414.16 |
| Authors | Pinheiro-Aguiar, R.,Amaral, V.S.G.,Bastos, I.,Kurtenbach, E.,Almeida, F.C.L. (deposition date: 2019-01-16, release date: 2019-08-21, Last modification date: 2024-10-23) |
| Primary citation | Pinheiro-Aguiar, R.,do Amaral, V.S.G.,Pereira, I.B.,Kurtenbach, E.,Almeida, F.C.L. Nuclear magnetic resonance solution structure of Pisum sativum defensin 2 provides evidence for the presence of hydrophobic surface-clusters. Proteins, 88:242-246, 2020 Cited by PubMed Abstract: 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 (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. PubMed: 31294889DOI: 10.1002/prot.25783 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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