The solution structure of human erythropoietin (EPO) has been determined by nuclear magnetic resonance spectroscopy and the overall topology of the protein is revealed as a novel combination of features taken from both the long-chain and short-chain families of hematopoietic growth factors. Using the structure and data from mutagenesis studies we have elucidated the key physiochemical properties defining each of the two receptor binding sites on the EPO protein. A comparison of the NMR structure of the free EPO ligand to the receptor bound form, determined by X-ray crystallography, reveals conformational changes that may accompany receptor binding.
Development of Non-Peptide Ligands of Growth Factor Receptor-Bound Protein 2-Src Homology 2 Domain Using Molecular Modeling and NMR Spectroscopy (†).
Development of Non-Peptide Ligands of Growth Factor Receptor-Bound Protein 2-Src Homology 2 Domain Using Molecular Modeling and NMR Spectroscopy (†).
Development of Non-Peptide Ligands of Growth Factor Receptor-Bound Protein 2-Src Homology 2 Domain Using Molecular Modeling and NMR Spectroscopy (†).
J Med Chem. 2011 Jan 27;
Authors: Orcajo-Rinco?n AL, Ortega-Gutie?rrez S, Serrano P, Torrecillas IR, Wu?thrich K, Campillo M, Pardo L, Viso A, Benhamu? B, Lo?pez-Rodri?guez ML
We report a novel series of non-peptide ligands that inhibit the growth...
[NMR paper] Solution NMR spectroscopy of the human vasopressin V2 receptor, a G protein-coupled r
Solution NMR spectroscopy of the human vasopressin V2 receptor, a G protein-coupled receptor.
Related Articles Solution NMR spectroscopy of the human vasopressin V2 receptor, a G protein-coupled receptor.
J Am Chem Soc. 2005 Jun 8;127(22):8010-1
Authors: Tian C, Breyer RM, Kim HJ, Karra MD, Friedman DB, Karpay A, Sanders CR
The seven-transmembrane-spanning G protein-coupled receptor (GPCR) superfamily plays many important roles in basic biology, human health, and human disease. Here, well-resolved solution NMR spectra are presented for a human...
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[NMR paper] Conformational changes in the human estrogen receptor observed by (19)F NMR.
Conformational changes in the human estrogen receptor observed by (19)F NMR.
Related Articles Conformational changes in the human estrogen receptor observed by (19)F NMR.
Biochem Biophys Res Commun. 2000 Apr 21;270(3):988-91
Authors: Luck LA, Barse JL, Luck AM, Peck CH
The (19)F NMR spectra of the 5F-Trp labeled glutathione-S-transferase fusion protein with residues 282-595 of the human estrogen receptor show that there is a distinct conformational change in the protein when estradiol is added to the unliganded protein. Our studies show the...
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11-18-2010 09:15 PM
[NMR paper] NMR solution structure of the receptor binding domain of human alpha(2)-macroglobulin
NMR solution structure of the receptor binding domain of human alpha(2)-macroglobulin.
Related Articles NMR solution structure of the receptor binding domain of human alpha(2)-macroglobulin.
J Biol Chem. 2000 Jan 14;275(2):1089-94
Authors: Huang W, Dolmer K, Liao X, Gettins PG
Human alpha(2)-macroglobulin-proteinase complexes bind to their receptor, the low density lipoprotein receptor-related protein (LRP), through a discrete 138-residue C-terminal receptor binding domain (RBD), which also binds to the beta-amyloid peptide. We have used NMR...
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[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] The structure of the human retinoic acid receptor-beta DNA-binding domain determined
The structure of the human retinoic acid receptor-beta DNA-binding domain determined by NMR.
Related Articles The structure of the human retinoic acid receptor-beta DNA-binding domain determined by NMR.
Nucleic Acids Symp Ser. 1992;(27):65-6
Authors: Katahira M, Knegtel R, Schilthius J, Boelens R, Eib D, van der Saag P, Kaptein R
The solution structure of the DNA-binding domain (DBD) of the human retinoic acid receptor-beta (hRAR-beta) has been determined by nuclear magnetic resonance (NMR) spectroscopy and distance geometry (DG). The...
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[NMR paper] NMR and ESR studies on human pregnancy zone protein. Comparison with human alpha 2-ma
NMR and ESR studies on human pregnancy zone protein. Comparison with human alpha 2-macroglobulin.
Related Articles NMR and ESR studies on human pregnancy zone protein. Comparison with human alpha 2-macroglobulin.
J Biol Chem. 1990 May 5;265(13):7268-72
Authors: Gettins P, Sottrup-Jensen L
NMR and ESR spectroscopies have been used to examine the plasma protease inhibitor pregnancy zone protein (PZP) and its complex with chymotrypsin. The 1H NMR spectrum of PZP shows relatively few sharp resonances, which, by analogy with human alpha...
NMR structure of human erythropoietin and a comparison with its receptor bound confor
Linear Mode
