Peptide hormone binding to G-protein-coupled receptors: Structural characterization via NMR techniques

2001 ◽  
Vol 21 (5) ◽  
pp. 450-471 ◽  
Author(s):  
Dale F. Mierke ◽  
Craig Giragossian
Keyword(s):  
G Protein ◽  
Structural Characterization ◽  
Peptide Hormone ◽  
G Protein Coupled Receptors ◽  
Hormone Binding ◽  
Nmr Techniques ◽  
G Protein Coupled

Extracellular loops and ligand binding to a subfamily of Family A G-protein-coupled receptors

2007 ◽  
Vol 35 (4) ◽  
pp. 717-720 ◽  
Author(s):  
M. Wheatley ◽  
J. Simms ◽  
S.R. Hawtin ◽  
V.J. Wesley ◽  
D. Wootten ◽  
...  
Keyword(s):  
Ligand Binding ◽  
G Protein ◽  
Tertiary Structure ◽  
Large Family ◽  
Peptide Hormone ◽  
Receptor Activation ◽  
G Protein Coupled Receptors ◽  
Ligand Selectivity ◽  
Extracellular Loops ◽  
G Protein Coupled

GPCRs (G-protein-coupled receptors) are a large family of structurally related proteins which mediate their effects by coupling to G-proteins. The V1aR (V1a vasopressin receptor) is a member of a family of related GPCRs that are activated by vasopressin {AVP ([Arg8]vasopressin)}, OT (oxytocin) and related peptides. These receptors are members of a subfamily of Family A GPCRs called the neurohypophysial peptide hormone receptor family. GPCRs exhibit a conserved tertiary structure comprising a bundle of seven TM (transmembrane) helices linked by alternating ECLs (extracellular loops) and ICLs (intracellular loops). The cluster of TM helices is functionally important for ligand binding, and, furthermore, activation of GPCRs involves movement of these TM helices. Consequently, it might be assumed that the extracellular face of GPCRs is composed of peptide linkers that merely connect important TM helices. However, using a systematic mutagenesis approach and focusing on the N-terminus and the second ECL of the V1aR, we have established that these extracellular domains fulfil a range of important roles with respect to GPCR signalling, including agonist binding, ligand selectivity and receptor activation.

scholarly journals NMR structure and peptide hormone binding site of the first extracellular domain of a type B1 G protein-coupled receptor

2004 ◽  
Vol 101 (35) ◽  
pp. 12836-12841 ◽  
Author(s):  
C. R. R. Grace ◽  
M. H. Perrin ◽  
M. R. DiGruccio ◽  
C. L. Miller ◽  
J. E. Rivier ◽  
...  
Keyword(s):  
Binding Site ◽  
G Protein ◽  
Peptide Hormone ◽  
Extracellular Domain ◽  
Nmr Structure ◽  
Hormone Binding ◽  
G Protein Coupled Receptor ◽  
G Protein Coupled
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