2M6A

NMR spatial structure of the antimicrobial peptide Tk-Amp-X2

Summary for 2M6A

• Entry DOI: 10.2210/pdb2m6a/pdb
• NMR Information: BMRB: 19124
• Descriptor: Predicted protein (1 entity in total)
• Functional Keywords: antimicrobial protein
• Biological source: Hordeum vulgare subsp. vulgare (barley,two-rowed barley)
• Total number of polymer chains: 1
• Total formula weight: 3533.10

Authors

Usmanova, D.R.,Mineev, K.S.,Arseniev, A.S.,Berkut, A.A.,Oparin, P.B.,Grishin, E.V.,Vassilevski, A.A. (deposition date: 2013-03-28, release date: 2014-04-02, Last modification date: 2024-10-30)

Primary citation

Berkut, A.A.,Usmanova, D.R.,Peigneur, S.,Oparin, P.B.,Mineev, K.S.,Odintsova, T.I.,Tytgat, J.,Arseniev, A.S.,Grishin, E.V.,Vassilevski, A.A.
Structural similarity between defense peptide from wheat and scorpion neurotoxin permits rational functional design
J.Biol.Chem., 289:14331-14340, 2014

PubMed Abstract: In this study, we present the spatial structure of the wheat antimicrobial peptide (AMP) Tk-AMP-X2 studied using NMR spectroscopy. This peptide was found to adopt a disulfide-stabilized α-helical hairpin fold and therefore belongs to the α-hairpinin family of plant defense peptides. Based on Tk-AMP-X2 structural similarity to cone snail and scorpion potassium channel blockers, a mutant molecule, Tk-hefu, was engineered by incorporating the functionally important residues from κ-hefutoxin 1 onto the Tk-AMP-X2 scaffold. The designed peptide contained the so-called essential dyad of amino acid residues significant for channel-blocking activity. Electrophysiological studies showed that although the parent peptide Tk-AMP-X2 did not present any activity against potassium channels, Tk-hefu blocked Kv1.3 channels with similar potency (IC50 ∼ 35 μm) to κ-hefutoxin 1 (IC50 ∼ 40 μm). We conclude that α-hairpinins are attractive in their simplicity as structural templates, which may be used for functional engineering and drug design.

PubMed: 24671422
DOI: 10.1074/jbc.M113.530477

Experimental method

SOLUTION NMR