Molecular basis of G protein-coupled receptor high affinity for gastrin-releasing peptide (GRP)

2003 ◽  
Vol 124 (4) ◽  
pp. A469
Author(s):  
Tomoo Nakagawa ◽  
Jose A. Tapia ◽  
Kenji Tokita ◽  
Samuel Mantey ◽  
Michael Schumann ◽  
...  
Keyword(s):  
G Protein ◽  
Molecular Basis ◽  
G Protein Coupled Receptor ◽  
Gastrin Releasing Peptide ◽  
High Affinity ◽  
G Protein Coupled

scholarly journals Molecular basis for the evolved instability of a human G-protein coupled receptor

Cell Reports ◽  
2021 ◽  
Vol 37 (8) ◽  
pp. 110046
Author(s):  
Laura M. Chamness ◽  
Nathan B. Zelt ◽  
Haley R. Harrington ◽  
Charles P. Kuntz ◽  
Brian J. Bender ◽  
...  
Keyword(s):  
G Protein ◽  
Molecular Basis ◽  
G Protein Coupled Receptor ◽  
G Protein Coupled

scholarly journals Molecular basis for activation of G protein-coupled receptor kinases

2010 ◽  
Vol 29 (19) ◽  
pp. 3249-3259 ◽  
Author(s):  
Cassandra A Boguth ◽  
Puja Singh ◽  
Chih-chin Huang ◽  
John J G Tesmer
Keyword(s):  
G Protein ◽  
Molecular Basis ◽  
G Protein Coupled Receptor ◽  
Receptor Kinases ◽  
G Protein Coupled

scholarly journals Molecular basis for high affinity agonist binding in GPCRs

2018 ◽  
Author(s):  
Tony Warne ◽  
Patricia C. Edwards ◽  
Andrew S. Doré ◽  
Andrew G. W. Leslie ◽  
Christopher G. Tate
Keyword(s):  
Hydrogen Bonds ◽  
Binding Site ◽  
G Protein ◽  
Molecular Basis ◽  
Agonist Binding ◽  
High Affinity ◽  
Protein Ligand Interactions ◽  
Wide Range ◽  
Ligand Interactions ◽  
G Protein Coupled

AbstractA characteristic of GPCRs in the G protein-coupled state is that the affinity of the agonist often increases significantly, but the molecular basis for this is unclear. We have determined six active-state structures of the β1-adrenoceptor (β1AR) bound to conformation-specific nanobodies in the presence of agonists of varying efficacy. A direct comparison with structures of β1AR in inactive states bound to the identical ligands showed a 24-42% reduction in the volume of the orthosteric binding site. Potential hydrogen bonds were also shorter, and there was up to a 30% increase in the number of atomic contacts between the receptor and ligand. GPCRs are highly conserved, so these factors will likely be essential in increasing the affinity of a wide range of structurally distinct agonists.One Sentence SummaryHigh affinity agonist binding to G protein-coupled GPCRs results from an increase in the number and strength of protein-ligand interactions.

A high-affinity peptide substrate for G protein-coupled receptor kinase 2 (GRK2)

Amino Acids ◽  
2019 ◽  
Vol 51 (6) ◽  
pp. 973-976
Author(s):  
Daisuke Asai ◽  
Masaharu Murata ◽  
Riki Toita ◽  
Takahito Kawano ◽  
Hideki Nakashima ◽  
...  
Keyword(s):  
G Protein ◽  
Receptor Kinase ◽  
Peptide Substrate ◽  
G Protein Coupled Receptor ◽  
High Affinity ◽  
Affinity Peptide ◽  
G Protein Coupled

scholarly journals Urotensin-II peptidomimetic incorporating a non-reducible 1,5-triazole disulfide bond reveals a pseudo-irreversible covalent binding mechanism to the urotensin G-protein coupled receptor

2017 ◽  
Vol 15 (21) ◽  
pp. 4704-4710 ◽  
Author(s):  
Salvatore Pacifico ◽  
Aidan Kerckhoffs ◽  
Andrew J. Fallow ◽  
Rachel E. Foreman ◽  
Remo Guerrini ◽  
...  
Keyword(s):  
G Protein ◽  
Disulfide Bond ◽  
Covalent Binding ◽  
Urotensin Ii ◽  
Binding Mechanism ◽  
G Protein Coupled Receptor ◽  
High Affinity ◽  
G Protein Coupled ◽  
Insight Into

New high affinity peptidomimetic ligands have been developed that provided new insight into the mechanism of binding of U-II peptide with the urotensin-II receptor.

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