Related ArticlesStructural characterization of peptide hormone/receptor interactions by NMR spectroscopy.
Biopolymers. 1999;51(3):208-20
Authors: Pellegrini M, Mierke DF
The structural characterization of peptide hormones and their interaction with G-protein (guanine nucleotide-binding regulatory protein) coupled receptors by high-resolution nmr is described. The general approaches utilized can be categorized into three different classes based on their target: the ligand, the receptor, and the ligand/receptor complex. Examples of these different approaches, aimed at facilitating the rational design of peptides and peptidomimetics with improved pharmacological profiles, based on work carried out in our own laboratory, are given. In the ligand-based approach, the high-resolution structures of bradykinin analogues allowing for the development of a structure-activity relationship for activation of the B1 receptor are described. Studies targeting the receptor are to a large extent theoretical, based on computational molecular modeling. However, experimentally based structural features provided by high-resolution nmr can be used to great advantage, providing insight into the mechanism of receptor function, as illustrated here with results from parathyroid hormone. A similar combination of theoretical methods, supplemented by high-resolution structures from nmr has been utilized to probe the formation and stabilization of the ligand/receptor complex both for parathyroid hormone and cholecystokinin. In each of these three approaches, the importance of well-designed peptide mimetics and accurate structural analysis by high-resolution nmr, will be highlighted.
Transferred NOESY NMR studies of biotin mimetic peptide (FSHPQNT) bound to streptavidin: A structural model for studies of peptide-protein interactions.
Transferred NOESY NMR studies of biotin mimetic peptide (FSHPQNT) bound to streptavidin: A structural model for studies of peptide-protein interactions.
Transferred NOESY NMR studies of biotin mimetic peptide (FSHPQNT) bound to streptavidin: A structural model for studies of peptide-protein interactions.
Chem Biol Drug Des. 2011 Feb 5;
Authors: Gizachew D, Dratz E
Protein-protein interactions control signaling, specific adhesion and many other biological functions. The three dimensional structures of the interfaces and bound ligand can be...
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[NMR paper] NMR structure and peptide hormone binding site of the first extracellular domain of a
NMR structure and peptide hormone binding site of the first extracellular domain of a type B1 G protein-coupled receptor.
Related Articles NMR structure and peptide hormone binding site of the first extracellular domain of a type B1 G protein-coupled receptor.
Proc Natl Acad Sci U S A. 2004 Aug 31;101(35):12836-41
Authors: Grace CR, Perrin MH, DiGruccio MR, Miller CL, Rivier JE, Vale WW, Riek R
The corticotropin-releasing factor (CRF) ligand family has diverse effects on the CNS, including the modulation of the stress response. The ligands'...
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[NMR paper] NMR-based structural characterization of large protein-ligand interactions.
NMR-based structural characterization of large protein-ligand interactions.
Related Articles NMR-based structural characterization of large protein-ligand interactions.
J Biomol NMR. 2002 Feb;22(2):165-73
Authors: Pellecchia M, Meininger D, Dong Q, Chang E, Jack R, Sem DS
Genomic research on target identification and validation has created a great need for methods that rapidly provide detailed structural information on protein-ligand interactions. We developed a suite of NMR experiments as rapid and efficient tools to provide descriptive...
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11-24-2010 08:49 PM
[NMR paper] Peptide hormone binding to G-protein-coupled receptors: structural characterization v
Peptide hormone binding to G-protein-coupled receptors: structural characterization via NMR techniques.
Related Articles Peptide hormone binding to G-protein-coupled receptors: structural characterization via NMR techniques.
Med Res Rev. 2001 Sep;21(5):450-71
Authors: Mierke DF, Giragossian C
G-protein-coupled receptors (GPCRs) allow cells to respond to calcium, hormones, and neurotransmitters. Not surprisingly, they currently make up the largest family of validated drug targets. Rational drug design for molecular regulators targeting GPCRs...
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11-19-2010 08:44 PM
[NMR paper] NMR structure of a receptor-bound G-protein peptide.
NMR structure of a receptor-bound G-protein peptide.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.nature.com-images-lo_nature.gif Related Articles NMR structure of a receptor-bound G-protein peptide.
Nature. 1993 May 20;363(6426):276-81
Authors: Dratz EA, Furstenau JE, Lambert CG, Thireault DL, Rarick H, Schepers T, Pakhlevaniants S, Hamm HE
Heterotrimeric GTP-binding proteins (G proteins) regulate cellular activity by coupling to hormone or sensory receptors. Stimulated receptors catalyse the release of GDP from G protein...
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08-21-2010 11:53 PM
[NMR paper] Structural characterization of a 39-residue synthetic peptide containing the two zinc
Structural characterization of a 39-residue synthetic peptide containing the two zinc binding domains from the HIV-1 p7 nucleocapsid protein by CD and NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Structural characterization of a 39-residue synthetic peptide containing the two zinc binding domains from the HIV-1 p7 nucleocapsid protein by CD and NMR spectroscopy.
FEBS Lett. 1991 Nov 4;292(1-2):25-30
Authors: Omichinski JG, Clore GM, Sakaguchi K, Appella E,...
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08-21-2010 11:12 PM
[NMR paper] Structural characterization of a 39-residue synthetic peptide containing the two zinc
Structural characterization of a 39-residue synthetic peptide containing the two zinc binding domains from the HIV-1 p7 nucleocapsid protein by CD and NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Structural characterization of a 39-residue synthetic peptide containing the two zinc binding domains from the HIV-1 p7 nucleocapsid protein by CD and NMR spectroscopy.
FEBS Lett. 1991 Nov 4;292(1-2):25-30
Authors: Omichinski JG, Clore GM, Sakaguchi K, Appella E,...
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[NMR paper] Structural characterization of the interactions of optimized product inhibitors with
Structural characterization of the interactions of optimized product inhibitors with the N-terminal proteinase domain of the hepatitis C virus (HCV) NS3 protein by NMR and modelling studies.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Structural characterization of the interactions of optimized product inhibitors with the N-terminal proteinase domain of the hepatitis C virus (HCV) NS3 protein by NMR and modelling studies.
J Mol Biol. 1999 Jun 4;289(2):385-96
Authors: Cicero...
Structural characterization of peptide hormone/receptor interactions by NMR spectrosc
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