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2NB6

NMR solution structure of PawS Derived Peptide 10 (PDP-10)

Summary for 2NB6
Entry DOI10.2210/pdb2nb6/pdb
Related2NB5
NMR InformationBMRB: 25963
DescriptorPreproalbumin PawS1 (1 entity in total)
Functional Keywordsplant peptide, plant protein
Biological sourceGalinsoga quadriradiata (Shaggy soldier)
Total number of polymer chains1
Total formula weight1817.05
Authors
Franke, B.G.,Elliott, A.G.,Mylne, J.S.,Rosengren, K.J. (deposition date: 2016-01-24, release date: 2016-06-29, Last modification date: 2024-11-20)
Primary citationElliott, A.G.,Franke, B.,Armstrong, D.A.,Craik, D.J.,Mylne, J.S.,Rosengren, K.J.
Natural structural diversity within a conserved cyclic peptide scaffold.
Amino Acids, 49:103-116, 2017
Cited by
PubMed Abstract: We recently isolated and described the evolutionary origin of a diverse class of small single-disulfide bonded peptides derived from Preproalbumin with SFTI-1 (PawS1) proteins in the seeds of flowering plants (Asteraceae). The founding member of the PawS derived peptide (PDP) family is the potent trypsin inhibitor SFTI-1 (sunflower trypsin inhibitor-1) from Helianthus annuus, the common sunflower. Here we provide additional structures and describe the structural diversity of this new class of small peptides, derived from solution NMR studies, in detail. We show that although most have a similar backbone framework with a single disulfide bond and in many cases a head-to-tail cyclized backbone, they all have their own characteristics in terms of projections of side-chains, flexibility and physiochemical properties, attributed to the variety of their sequences. Small cyclic and constrained peptides are popular as drug scaffolds in the pharmaceutical industry and our data highlight how amino acid side-chains can fine-tune conformations in these promising peptides.
PubMed: 27695949
DOI: 10.1007/s00726-016-2333-x
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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