PURPOSE: Vitamin A (retinol) and its metabolites comprise the natural retinoids. While the biological action of these molecules are thought to be primarily mediated by ca. 55 kDa nuclear retinoic acid receptors, a number of structurally similar 15-20 kDa proteins are involved in the transport, and possibly metabolism, of these compounds. The milk protein beta-lactoglobulin B (beta-LG) is an 18 kDa protein which binds retinol and may be involved in oral delivery of retinol to neonates. beta-LG also binds drugs and other natural products and is of potential interest as a protective delivery vehicle. METHODS: To examine the conformation of the model retinoid beta-ionone both in solution and when bound to beta-LG, NMR and computational methods have been employed. RESULTS: Taken together, NMR studies of beta-ionone in solution measuring scalar and dipolar coupling, as well as CHARMm calculations, suggest beta-ionone prefers a slightly twisted 6-s-cis conformation. Isotope-edited NMR studies of 13C-labeled beta-ionones bound to beta-LG, primarily employing the HMQC-NOE experiment, suggest beta-ionone also binds to beta-LG in its 6-s-cis conformation. CONCLUSIONS: The methods employed here allow estimates of protein-bound ligand conformation. However, additional sites of ligand labeling will be necessary to aid in binding site localization.
[NMR paper] NMR studies for identifying phosphopeptide ligands of the HIV-1 protein Vpu binding to the F-box protein beta-TrCP.
NMR studies for identifying phosphopeptide ligands of the HIV-1 protein Vpu binding to the F-box protein beta-TrCP.
Related Articles NMR studies for identifying phosphopeptide ligands of the HIV-1 protein Vpu binding to the F-box protein beta-TrCP.
Peptides. 2006 Jan;27(1):194-210
Authors: Evrard-Todeschi N, Gharbi-Benarous J, Bertho G, Coadou G, Megy S, Benarous R, Girault JP
The human immunodeficiency virus type 1 (HIV-1) Vpu enhances viral particle release and, its interaction with the ubiquitin ligase SCF-beta-TrCP triggers the HIV-1...
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[NMR paper] Cell-free protein synthesis in an autoinduction system for NMR studies of protein-protein interactions.
Cell-free protein synthesis in an autoinduction system for NMR studies of protein-protein interactions.
Related Articles Cell-free protein synthesis in an autoinduction system for NMR studies of protein-protein interactions.
J Biomol NMR. 2005 Jul;32(3):235-41
Authors: Ozawa K, Jergic S, Crowther JA, Thompson PR, Wijffels G, Otting G, Dixon NA
Cell-free protein synthesis systems provide facile access to proteins in a nascent state that enables formation of soluble, native protein-protein complexes even if one of the protein components is prone...
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[NMR paper] STD and TRNOESY NMR studies on the conformation of the oncogenic protein beta-catenin
STD and TRNOESY NMR studies on the conformation of the oncogenic protein beta-catenin containing the phosphorylated motif DpSGXXpS bound to the beta-TrCP protein.
Related Articles STD and TRNOESY NMR studies on the conformation of the oncogenic protein beta-catenin containing the phosphorylated motif DpSGXXpS bound to the beta-TrCP protein.
J Biol Chem. 2005 Aug 12;280(32):29107-16
Authors: Megy S, Bertho G, Gharbi-Benarous J, Evrard-Todeschi N, Coadou G, Ségéral E, Iehle C, Quéméneur E, Benarous R, Girault JP
beta-TrCP is the F-box protein...
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[NMR paper] NMR studies of restriction enzyme-DNA interactions: role of conformation in sequence
NMR studies of restriction enzyme-DNA interactions: role of conformation in sequence specificity.
Related Articles NMR studies of restriction enzyme-DNA interactions: role of conformation in sequence specificity.
Biochemistry. 2005 Apr 5;44(13):5065-74
Authors: Dupureur CM
Sequence specific DNA binding proteins are thought to adopt distinct conformations when binding to target (cognate) and nontarget (noncognate) sequences. There is both biochemical and crystallographic evidence that this behavior is important in mediating sequence recognition...
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[NMR paper] Conformation of a beta-adrenoceptor-derived signal transducing peptide as inferred by
Conformation of a beta-adrenoceptor-derived signal transducing peptide as inferred by circular dichroism and 1H NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Conformation of a beta-adrenoceptor-derived signal transducing peptide as inferred by circular dichroism and 1H NMR spectroscopy.
Biochemistry. 1996 May 21;35(20):6399-405
Authors: Jung H, Windhaber R, Palm D, Schnackerz KD
The peptide T345-359 representing the fourth intracellular loop of the avian...
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08-22-2010 02:27 PM
[NMR paper] 1H-NMR spectroscopy of beta B2-crystallin from bovine eye lens. Conformation of the N
1H-NMR spectroscopy of beta B2-crystallin from bovine eye lens. Conformation of the N- and C-terminal extensions.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles 1H-NMR spectroscopy of beta B2-crystallin from bovine eye lens. Conformation of the N- and C-terminal extensions.
Eur J Biochem. 1993 Apr 1;213(1):313-20
Authors: Carver JA, Cooper PG, Truscott RJ
1H-NMR spectroscopic studies of a 46-kDa homodimer, beta B2-crystallin,...
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[NMR paper] The solution conformation of tubulin-beta(422-434)-NH2 and its Nac-DATADEQG-NH2 fragm
The solution conformation of tubulin-beta(422-434)-NH2 and its Nac-DATADEQG-NH2 fragment based on NMR.
Related Articles The solution conformation of tubulin-beta(422-434)-NH2 and its Nac-DATADEQG-NH2 fragment based on NMR.
Biopolymers. 1991 Mar;31(4):449-58
Authors: Otter A, Scott PG, Maccioni RB, Kotovych G
The solution conformation of tubulin-beta(422-434)-NH2 (YQQYQDATADEQG-NH2) and its Nac-DATADEQG-NH2 fragment has been studied by two-dimensional 1H-nmr spectroscopy in CD3OH/H2O (90/10 v/v) at neutral and low pH. The 13 amino acid peptide...