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Endothelin and Its Receptor Interactions: Role of Extracellular Receptor Domain and Length of Peptide Ligands

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Human endothelin B receptor and its domain-truncated forms were cloned and expressed in Pichia pastoris. Ligand binding studies with expressed proteins were carried out using biotinylated endothelins. Competitive binding and liposome incorporation studies showed that the extracellular region is essential for ligand binding and that longer peptides have higher affinity.

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Keywords: Pichia expression; Recombinant human endothelin B receptors; competitive binding; synthetic peptides

Document Type: Research Article

Publication date: 2007-08-01

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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