Related ArticlesChanges in the NMR-derived motional parameters of the insulin receptor substrate 1 phosphotyrosine binding domain upon binding to an interleukin 4 receptor phosphopeptide.
Biochemistry. 1997 Apr 8;36(14):4118-24
Authors: Olejniczak ET, Zhou MM, Fesik SW
Proteins recognize ligands by forming specific intermolecular interactions that often involve solvent exposed residues. Changes in the motional properties of these residues upon binding can affect the conformational entropy of the system and thus are related to the energetics of binding. The role that dynamics plays in ligand recognition can be investigated by comparing the motional properties of a free and ligated protein. NMR relaxation studies are well suited for examining changes in dynamics, especially for motions on a nanosecond to picosecond time scale. Recently, we determined the solution structure of the phosphotyrosine binding (PTB) domain of the insulin receptor substrate (IRS-1) complexed to a tyrosine-phosphorylated peptide derived from the interleukin 4 (IL-4) receptor [Zhou et al., (1996) Nat. Struct. Biol. 3, 388-393]. The peptide binds tightly to the protein in a surface exposed pocket, resulting in the partial burial of many protein residues. Using NMR relaxation studies, the dynamics of the backbone nitrogens of IRS-1 PTB domain were studied in both the free protein and the protein when complexed to the IL-4 receptor phosphopeptide. The backbone nitrogens of many residues that make important contacts to the ligand are motionally restricted in the free and complexed protein. Additional residues become motionally restricted only after ligand binding, including several residues that do not make any direct contacts with the ligand. These observed changes in the dynamics are compared to structural features of the complex.
Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexes.
Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexes.
Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexes.
J Inorg Biochem. 2010 Oct;104(10):1063-70
Authors: Du Z, Unno M, Matsui T, Ikeda-Saito M, La Mar GN
Proton 2D NMR was used to confirm in solution a highly conserved portion of the molecular structure upon substrate loss for the...
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[NMR paper] The NMR-derived conformation of orexin-A: an orphan G-protein coupled receptor agonis
The NMR-derived conformation of orexin-A: an orphan G-protein coupled receptor agonist involved in appetite regulation and sleep.
Related Articles The NMR-derived conformation of orexin-A: an orphan G-protein coupled receptor agonist involved in appetite regulation and sleep.
J Biomol Struct Dyn. 2003 Oct;21(2):201-10
Authors: Miskolzie M, Kotovych G
The conformation of orexin-A, an orphan G-protein coupled receptor agonist has been determined when bound to sodium dodecylsulphate-d(25) (SDS) micelles by (1)H and (13)C NMR and molecular...
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[NMR paper] The NMR-derived conformation of neuropeptide AF, an orphan G-protein coupled receptor
The NMR-derived conformation of neuropeptide AF, an orphan G-protein coupled receptor peptide.
Related Articles The NMR-derived conformation of neuropeptide AF, an orphan G-protein coupled receptor peptide.
Biopolymers. 2003 Jun;69(2):201-15
Authors: Miskolzie M, Kotovych G
The tertiary structure of the pain modulating and anti-opiate neuropeptide, human neuropeptide AF (NPAF) (the sequence is AGEGLNSQFWSLAAPQRF-NH(2)), was determined by (1)H-NMR. The structure of NPAF was determined in two solvent systems, namely 50%/50%...
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[NMR paper] Changes in the NMR-derived motional parameters of the insulin receptor substrate 1 ph
Changes in the NMR-derived motional parameters of the insulin receptor substrate 1 phosphotyrosine binding domain upon binding to an interleukin 4 receptor phosphopeptide.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Changes in the NMR-derived motional parameters of the insulin receptor substrate 1 phosphotyrosine binding domain upon binding to an interleukin 4 receptor phosphopeptide.
Biochemistry. 1997 Apr 8;36(14):4118-24
Authors: Olejniczak ET, Zhou MM, Fesik SW
Proteins recognize...
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08-22-2010 03:03 PM
[NMR paper] Comparative 2D NMR studies of human insulin and des-pentapeptide insulin: sequential
Comparative 2D NMR studies of human insulin and des-pentapeptide insulin: sequential resonance assignment and implications for protein dynamics and receptor recognition.
Related Articles Comparative 2D NMR studies of human insulin and des-pentapeptide insulin: sequential resonance assignment and implications for protein dynamics and receptor recognition.
Biochemistry. 1991 Jun 4;30(22):5505-15
Authors: Hua QX, Weiss MA
The solution structure and dynamics of human insulin are investigated by 2D 1H NMR spectroscopy in reference to a previously...
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08-21-2010 11:16 PM
[NMR paper] Autophosphorylation of soluble insulin receptor protein-tyrosine kinases. 1H NMR spec
Autophosphorylation of soluble insulin receptor protein-tyrosine kinases. 1H NMR spectral changes observed during phosphorylation of mobile tyrosine residues.
Related Articles Autophosphorylation of soluble insulin receptor protein-tyrosine kinases. 1H NMR spectral changes observed during phosphorylation of mobile tyrosine residues.
J Biol Chem. 1991 Jul 15;266(20):13405-10
Authors: Levine BA, Tavaré JM, Alejos E, Clack B, Sayed N
Autophosphorylation of a soluble approximately 48-kDa derivative of the insulin receptor protein-tyrosine kinase...
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[NMR paper] Autophosphorylation of soluble insulin receptor protein-tyrosine kinases. 1H NMR spec
Autophosphorylation of soluble insulin receptor protein-tyrosine kinases. 1H NMR spectral changes observed during phosphorylation of mobile tyrosine residues.
Related Articles Autophosphorylation of soluble insulin receptor protein-tyrosine kinases. 1H NMR spectral changes observed during phosphorylation of mobile tyrosine residues.
J Biol Chem. 1991 Jul 15;266(20):13405-10
Authors: Levine BA, Tavaré JM, Alejos E, Clack B, Sayed N
Autophosphorylation of a soluble approximately 48-kDa derivative of the insulin receptor protein-tyrosine kinase...
Changes in the NMR-derived motional parameters of the insulin receptor substrate 1 ph
Linear Mode
