Endothelin and its receptor interactions: role of extracellular receptor domain and length of peptide ligands.
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.
Saravanan
K
K
Department of Biophysics, All India Institute of Medical Sciences, New Delhi, India.
Hariprasad
G
G
Jitesh
O
O
Das
U
U
Dey
S
S
Sharma
S
S
Kaur
P
P
Singh
T P
TP
Srinivasan
A
A
D000595:Amino Acid Sequence; D001667:Binding, Competitive; D019921:Biotinylation; D003001:Cloning, Molecular; D016232:Endothelins / Q000378:metabolism*; D005260:Female; D006801:Humans; D008024:Ligands; D008081:Liposomes / Q000378:metabolism; D010843:Pichia / Q000378:metabolism; D011247:Pregnancy; D017434:Protein Structure, Tertiary; D044023:Receptor, Endothelin B / Q000378:metabolism*
D016232:Endothelins; D008024:Ligands; D008081:Liposomes; D044023:Receptor, Endothelin B; C061778:endothelin 1, Ala(3,11)-