Related ArticlesNMR studies of the pbx1 TALE homeodomain protein free in solution and bound to DNA: proposal for a mechanism of HoxB1-Pbx1-DNA complex assembly.
J Mol Biol. 1999 Aug 20;291(3):521-30
Authors: Jabet C, Gitti R, Summers MF, Wolberger C
The Hox homeodomain proteins are transcription factors involved in developmental regulation. Many of the vertebrate Hox proteins bind DNA cooperatively with the Pbx1 homeodomain protein. The crystal structure of a human HoxB1-Pbx1-DNA ternary complex revealed that interactions between the two proteins are mediated by the HoxB1 hexapeptide, which inserts into a hydrophobic pocket in Pbx1. It was also found that the Pbx1 DNA-binding domain is larger than the canonical three-helix homeodomain, containing an additional alpha-helix that is joined to the C terminus of the homeodomain by a turn of 310helix. These extra C-terminal residues had previously been shown to augment the cooperative interaction of Pbx1 with Hox partners, as well as enhancing the DNA binding of monomeric Pbx1. In order to characterize the role of the fourth Pbx1 helix in greater detail, we have examined the backbone structure of the enlarged Pbx1 DNA-binding domain in solution by(1)H,(15)N and(13)C multidimensional NMR spectroscopy. Our results show that the additional alpha-helix of Pbx1 is unfolded when the protein is free in solution and that its folding is triggered by binding of Pbx1 to DNA. In contrast, no change in conformation is observed upon mixing the HoxB1 protein with Pbx1 in the absence of DNA. This study suggests a model for the assembly of a stable HoxB1-Pbx1-DNA ternary complex.
[MWClarkson blog] Dynamic origins of PBX1 homeodomain allostery
Dynamic origins of PBX1 homeodomain allostery
http://www.researchblogging.org/public/citation_icons/rb2_large_gray.pngIn the Monod-Wyman-Changeux model for cooperative binding, proteins exist in an equilibrium of low-affinity and high-affinity states in solution, absent any ligand. In this view, although it may appear that the binding of a ligand causes a conformational transition, it actually stabilizes one conformation from a pre-existing equilibrium. In the past several years, advanced NMR techniques have yielded increasing evidence that these structural equilibria exist for a number of...
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12-02-2010 08:41 AM
[NMR paper] 15N NMR relaxation studies of free and ligand-bound human acidic fibroblast growth fa
15N NMR relaxation studies of free and ligand-bound human acidic fibroblast growth factor.
Related Articles 15N NMR relaxation studies of free and ligand-bound human acidic fibroblast growth factor.
J Biol Chem. 2000 Dec 15;275(50):39444-50
Authors: Chi Y, Kumar TK, Chiu IM, Yu C
15N NMR relaxation data have been used to characterize the backbone dynamics of the human acidic fibroblast growth factor (hFGF-1) in its free and sucrose octasulfate (SOS)-bound states. (15)N longitudinal (R(1)), transverse (R(2)) relaxation rates and (1H)-(15)N...
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11-19-2010 08:29 PM
[NMR paper] The NMR solution structure of the non-classical homeodomain from the rat liver LFB1/H
The NMR solution structure of the non-classical homeodomain from the rat liver LFB1/HNF1 transcription factor.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles The NMR solution structure of the non-classical homeodomain from the rat liver LFB1/HNF1 transcription factor.
J Mol Biol. 1997 Apr 4;267(3):673-83
Authors: Schott O, Billeter M, Leiting B, Wider G, Wüthrich K
The nuclear magnetic resonance (NMR) solution structure of the non-classical homeodomain from the rat...
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08-22-2010 03:31 PM
[NMR paper] The NMR solution structure of the non-classical homeodomain from the rat liver LFB1/H
The NMR solution structure of the non-classical homeodomain from the rat liver LFB1/HNF1 transcription factor.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles The NMR solution structure of the non-classical homeodomain from the rat liver LFB1/HNF1 transcription factor.
J Mol Biol. 1997 Apr 4;267(3):673-83
Authors: Schott O, Billeter M, Leiting B, Wider G, Wüthrich K
The nuclear magnetic resonance (NMR) solution structure of the non-classical homeodomain from the rat...
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08-22-2010 03:03 PM
[NMR paper] 15N NMR relaxation studies of free and inhibitor-bound 4-oxalocrotonate tautomerase:
15N NMR relaxation studies of free and inhibitor-bound 4-oxalocrotonate tautomerase: backbone dynamics and entropy changes of an enzyme upon inhibitor binding.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles 15N NMR relaxation studies of free and inhibitor-bound 4-oxalocrotonate tautomerase: backbone dynamics and entropy changes of an enzyme upon inhibitor binding.
Biochemistry. 1996 Dec 17;35(50):16036-47
Authors: Stivers JT, Abeygunawardana C, Mildvan AS
The solution secondary...
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08-22-2010 02:20 PM
[NMR paper] 31P-NMR of free and protein-bound molybdopterin guanine dinucleotide.
31P-NMR of free and protein-bound molybdopterin guanine dinucleotide.
Related Articles 31P-NMR of free and protein-bound molybdopterin guanine dinucleotide.
Biofactors. 1992 Jan;3(3):197-200
Authors: Bastian NR, Johnson JL, Rajagopalan KV
Molybdopterin guanine dinucleotide was studied by 31P-NMR in the free, iodoacetamide derivatized form and in the native state in the dimethyl sulfoxide reductase from Rhodobacter sphaeroides. The spectra confirm the presence of a pyrophosphate moiety in the cofactor molecule. Comparison of the spectrum of...
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08-21-2010 11:41 PM
[NMR paper] NMR studies of [U-13C]cyclosporin A bound to cyclophilin: bound conformation and port
NMR studies of cyclosporin A bound to cyclophilin: bound conformation and portions of cyclosporin involved in binding.
Related Articles NMR studies of cyclosporin A bound to cyclophilin: bound conformation and portions of cyclosporin involved in binding.
Biochemistry. 1991 Jul 2;30(26):6574-83
Authors: Fesik SW, Gampe RT, Eaton HL, Gemmecker G, Olejniczak ET, Neri P, Holzman TF, Egan DA, Edalji R, Simmer R
Cyclosporin A (CsA), a potent immunosuppressant, is known to bind with high specificity to cyclophilin (CyP), a 17.7 kDa protein with...
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08-21-2010 11:12 PM
[NMR paper] NMR studies of [U-13C]cyclosporin A bound to cyclophilin: bound conformation and port
NMR studies of cyclosporin A bound to cyclophilin: bound conformation and portions of cyclosporin involved in binding.
Related Articles NMR studies of cyclosporin A bound to cyclophilin: bound conformation and portions of cyclosporin involved in binding.
Biochemistry. 1991 Jul 2;30(26):6574-83
Authors: Fesik SW, Gampe RT, Eaton HL, Gemmecker G, Olejniczak ET, Neri P, Holzman TF, Egan DA, Edalji R, Simmer R
Cyclosporin A (CsA), a potent immunosuppressant, is known to bind with high specificity to cyclophilin (CyP), a 17.7 kDa protein with...
NMR studies of the pbx1 TALE homeodomain protein free in solution and bound to DNA: p
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