Molecular Basis of Glucagon-like Peptide 1 Docking to Its Intact Receptor Studied with Carboxyl-terminal Photolabile Probes*
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Laurence J Miller | Maoqing Dong | L. Miller | M. Dong | D. Pinon | Delia I Pinon | Quan Chen | Quan Chen
[1] M. Wheeler,et al. Characterization of glucagon-like peptide-1 receptor-binding determinants. , 2000, Journal of molecular endocrinology.
[2] A. Couvineau,et al. Peptide Agonist Docking in the N-terminal Ectodomain of a Class II G Protein-coupled Receptor, the VPAC1 Receptor , 2006, Journal of Biological Chemistry.
[3] A. Couvineau,et al. The N-Terminal Parts of VIP and Antagonist PG97–269 Physically Interact with Different Regions of the Human VPAC1 Receptor , 2008, Journal of Molecular Neuroscience.
[4] D. Donnelly,et al. A model for receptor–peptide binding at the glucagon‐like peptide‐1 (GLP‐1) receptor through the analysis of truncated ligands and receptors , 2003, British journal of pharmacology.
[5] R. Riek,et al. NMR structure and peptide hormone binding site of the first extracellular domain of a type B1 G protein-coupled receptor. , 2004, Proceedings of the National Academy of Sciences of the United States of America.
[6] B. Göke,et al. Five Out of Six Tryptophan Residues in the N-Terminal Extracellular Domain of the Rat GLP-1 Receptor Are Essential for its Ability to Bind GLP-1 , 1997, Peptides.
[7] L. Miller,et al. Importance of the Amino Terminus in Secretin Family G Protein-coupled Receptors , 2004, Journal of Biological Chemistry.
[8] D. Donnelly,et al. Peptide binding at the GLP-1 receptor. , 2007, Biochemical Society transactions.
[9] K. Eckart,et al. Structure/activity characterization of glucagon-like peptide-1. , 1994, European journal of biochemistry.
[10] J. Vilardaga,et al. The C-terminus ends of secretin and VIP interact with the N-terminal domains of their receptors , 1996, Peptides.
[11] T. Lybrand,et al. Spatial approximation between a photolabile residue in position 13 of secretin and the amino terminus of the secretin receptor. , 2003, Molecular pharmacology.
[12] L. B. Knudsen,et al. Structure-activity studies of glucagon-like peptide-1. , 1994, The Journal of biological chemistry.
[13] H. Jüppner,et al. Identification of Determinants of Inverse Agonism in a Constitutively Active Parathyroid Hormone/Parathyroid Hormone-related Peptide Receptor by Photoaffinity Cross-linking and Mutational Analysis* , 2001, The Journal of Biological Chemistry.
[14] D. Gorenstein,et al. Structure of glucagon-like peptide (7-36) amide in a dodecylphosphocholine micelle as determined by 2D NMR. , 1994, Biochemistry.
[15] D. Donnelly,et al. Met-204 and Tyr-205 are together important for binding GLP-1 receptor agonists but not their N-terminally truncated analogues. , 2004, Protein and peptide letters.
[16] A. Couvineau,et al. The vasoactive intestinal peptide (VIP) alpha-Helix up to C terminus interacts with the N-terminal ectodomain of the human VIP/Pituitary adenylate cyclase-activating peptide 1 receptor: photoaffinity, molecular modeling, and dynamics. , 2008, Molecular endocrinology.
[17] Kjeld Madsen,et al. Crystal Structure of the Ligand-bound Glucagon-like Peptide-1 Receptor Extracellular Domain* , 2008, Journal of Biological Chemistry.
[18] H. Xu,et al. Molecular recognition of parathyroid hormone by its G protein-coupled receptor , 2008, Proceedings of the National Academy of Sciences.
[19] R. Stevens,et al. High-Resolution Crystal Structure of an Engineered Human β2-Adrenergic G Protein–Coupled Receptor , 2007, Science.
[20] L. Miller,et al. Use of N,O-bis-Fmoc-D-Tyr-ONSu for introduction of an oxidative iodination site into cholecystokinin family peptides. , 2009, International journal of peptide and protein research.
[21] T. Lybrand,et al. Direct Identification of a Distinct Site of Interaction between the Carboxyl-terminal Residue of Cholecystokinin and the Type A Cholecystokinin Receptor Using Photoaffinity Labeling* , 1997, The Journal of Biological Chemistry.
[22] Y. Cao,et al. The amino-terminal fragment of the adenylate cyclase activating polypeptide (PACAP) receptor functions as a high affinity PACAP binding domain. , 1995, Biochemical and biophysical research communications.
[23] T. Lybrand,et al. Spatial Approximation between the Amino Terminus of a Peptide Agonist and the Top of the Sixth Transmembrane Segment of the Secretin Receptor* , 2004, Journal of Biological Chemistry.
[24] Ruben Abagyan,et al. ICM—A new method for protein modeling and design: Applications to docking and structure prediction from the distorted native conformation , 1994, J. Comput. Chem..
[25] D Rodbard,et al. Ligand: a versatile computerized approach for characterization of ligand-binding systems. , 1980, Analytical biochemistry.
[26] R. Abagyan,et al. Molecular Approximations between Residues 21 and 23 of Secretin and Its Receptor: Development of a Model for Peptide Docking with the Amino Terminus of the Secretin Receptor , 2007, Molecular Pharmacology.
[27] L. Miller,et al. Molecular Approximation between a Residue in the Amino-terminal Region of Calcitonin and the Third Extracellular Loop of the Class B G Protein-coupled Calcitonin Receptor* , 2004, Journal of Biological Chemistry.
[28] L. Miller,et al. Critical Contributions of Amino-terminal Extracellular Domains in Agonist Binding and Activation of Secretin and Vasoactive Intestinal Polypeptide Receptors. STUDIES OF CHIMERIC RECEPTORS (*) , 1995, The Journal of Biological Chemistry.
[29] L. Miller,et al. Insights into the structural basis of endogenous agonist activation of family B G protein-coupled receptors. , 2008, Molecular endocrinology.
[30] J. W. Neidigh,et al. Exendin-4 and glucagon-like-peptide-1: NMR structural comparisons in the solution and micelle-associated states. , 2001, Biochemistry.
[31] L. Miller,et al. Relationship Between Native and Recombinant Cholecystokinin Receptors: Role of Differential Glycosylation , 1996, Pancreas.
[32] L. Miller,et al. Demonstration of a Direct Interaction between Residue 22 in the Carboxyl-terminal Half of Secretin and the Amino-terminal Tail of the Secretin Receptor Using Photoaffinity Labeling* , 1999, The Journal of Biological Chemistry.
[33] G. Bitan,et al. Photoaffinity Cross-linking Identifies Differences in the Interactions of an Agonist and an Antagonist with the Parathyroid Hormone/Parathyroid Hormone-related Protein Receptor* , 2000, The Journal of Biological Chemistry.
[34] R. Abagyan,et al. Spatial Approximation between Secretin Residue Five and the Third Extracellular Loop of Its Receptor Provides New Insight into the Molecular Basis of Natural Agonist Binding , 2008, Molecular Pharmacology.
[35] L. Suva,et al. Parathyroid Hormone-Receptor Interactions Identified Directly by Photocross-linking and Molecular Modeling Studies* , 1998, The Journal of Biological Chemistry.
[36] B. Gallwitz,et al. GLP-1 GIP chimeric peptides define the structural requirements for specific ligand-receptor interaction of GLP-1 , 1996, Regulatory Peptides.
[37] Oliver P. Ernst,et al. Crystal structure of opsin in its G-protein-interacting conformation , 2008, Nature.
[38] J. Livingston,et al. Glucagon·Glucagon-like Peptide I Receptor Chimeras Reveal Domains That Determine Specificity of Glucagon Binding (*) , 1995, The Journal of Biological Chemistry.
[39] H. Xu,et al. Molecular Recognition of Corticotropin-releasing Factor by Its G-protein-coupled Receptor CRFR1* , 2008, Journal of Biological Chemistry.
[40] D. Singleton,et al. Structure-function analysis of a series of glucagon-like peptide-1 analogs. , 2009, The journal of peptide research : official journal of the American Peptide Society.
[41] C. Strader,et al. The amino terminal domain of the glucagon-like peptide-1 receptor is a critical determinant of subtype specificity. , 1996, Receptors & channels.
[42] Renxiao Wang,et al. Molecular modeling of the three-dimensional structure of GLP-1R and its interactions with several agonists , 2009, Journal of molecular modeling.
[43] R. Stevens,et al. The 2.6 Angstrom Crystal Structure of a Human A2A Adenosine Receptor Bound to an Antagonist , 2008, Science.
[44] B. Wulff,et al. Different domains of the glucagon and glucagon‐like peptide‐1 receptors provide the critical determinants of ligand selectivity , 2003, British journal of pharmacology.
[45] P. Hajduk,et al. Solution structure and mutational analysis of pituitary adenylate cyclase-activating polypeptide binding to the extracellular domain of PAC1-RS , 2007, Proceedings of the National Academy of Sciences.
[46] N. Andersen,et al. Medium-dependence of the secondary structure of exendin-4 and glucagon-like-peptide-1. , 2002, Bioorganic & medicinal chemistry.
[47] H. Jüppner,et al. Evidence for a Ligand Interaction Site at the Amino-Terminus of the Parathyroid Hormone (PTH)/PTH-related Protein Receptor from Cross-linking and Mutational Studies* , 1998, The Journal of Biological Chemistry.
[48] H. Jüppner,et al. Multiple Sites of Contact between the Carboxyl-terminal Binding Domain of PTHrP-(1–36) Analogs and the Amino-terminal Extracellular Domain of the PTH/PTHrP Receptor Identified by Photoaffinity Cross-linking* , 2001, Journal of Biological Chemistry.
[49] L. Miller,et al. Intrinsic photoaffinity labeling of native and recombinant rat pancreatic secretin receptors. , 1993, Gastroenterology.
[50] R. Riek,et al. Structure of the N-terminal domain of a type B1 G protein-coupled receptor in complex with a peptide ligand , 2007, Proceedings of the National Academy of Sciences.
[51] R. Rudolph,et al. Crystal structure of the incretin-bound extracellular domain of a G protein-coupled receptor , 2007, Proceedings of the National Academy of Sciences.