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Structure-function analyses reveal a triple ß-turn receptor-bound conformation of adrenomedullin 2/intermedin and enable peptide antagonist design.
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Structure-function analyses reveal a triple ß-turn receptor-bound conformation of adrenomedullin 2/intermedin and enable peptide antagonist design.
Structure-function analyses reveal a triple ß-turn receptor-bound conformation of adrenomedullin 2/intermedin and enable peptide antagonist design. J Biol Chem. 2018 10 12; 293(41):15840-15854.
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PubMed
subject areas
Adrenomedullin
Adrenomedullin
Calcitonin Gene-Related Peptide
Calcitonin Gene-Related Peptide
Calcitonin Receptor-Like Protein
Calcitonin Receptor-Like Protein
Drug Design
Drug Design
HEK293 Cells
HEK293 Cells
Humans
Humans
Ligands
Ligands
Mutagenesis, Site-Directed
Mutagenesis, Site-Directed
Peptide Hormones
Peptide Hormones
Protein Binding
Protein Binding
Protein Conformation
Protein Conformation
Protein Engineering
Protein Engineering
Receptor Activity-Modifying Protein 1
Receptor Activity-Modifying Protein 1
Receptor Activity-Modifying Protein 2
Receptor Activity-Modifying Protein 2
Receptor Activity-Modifying Protein 3
Receptor Activity-Modifying Protein 3
Receptor Activity-Modifying Proteins
Receptor Activity-Modifying Proteins
Receptors, Adrenomedullin
Receptors, Adrenomedullin
authors with profiles
Augen A Pioszak