ArticleChembiochem : a European journal of chemical biology2014
Conformational flexibility in the binding surface of the potassium channel blocker ShK.
Article in Chembiochem : a European journal of chemical biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Article
- Bioproduction Platform to Generate Functionalized Disulfide-Constrained Peptide Analogues.ACS bio & med chem Au · 2024Article
- Structure of the voltage-gated potassium channel KChannels (Austin, Tex.) · 2023Review
- Removing Thermostat Distortions of Protein Dynamics in Constant-Temperature Molecular Dynamics Simulations.Journal of chemical theory and computation · 2021Article
- Conformational exchange in the potassium channel blocker ShK.Scientific reports · 2019Article
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Authors and funding
7 authors.
Funding
Abstract
ShK is a 35-residue peptide that binds with high affinity to human voltage-gated potassium channels through a conserved K-Y dyad. Here we have employed NMR measurements of backbone-amide (15)N spin-relaxation rates to investigate motions of the ShK backbone. Although ShK is rigid on the ps to ns timescale, increased linewidths observed for 11 backbone-amide (15)N resonances identify chemical or conformational exchange contributions to the spin relaxation. Relaxation dispersion profiles indicate that exchange between major and minor conformers occurs on the sub-millisecond timescale. Affected residues are mostly clustered around the central helix-kink-helix structure and the critical K22-Y23 motif. We suggest that the less structured minor conformer increases the exposure of Y23, known to contribute to binding affinity and selectivity, thereby facilitating its interaction with potassium channels. These findings have potential implications for the design of new channel blockers based on ShK.
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