Related ArticlesThe 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 assignments of 1H and 15N resonances were carried out by the use of 1H homonuclear and 15N-1H heteronuclear two- and three-dimensional NMR experiments. The structure of RAR DBD has been obtained on the basis of distance constrains derived from NMR experiments. The structure shows that two "zinc-finger" domains of the protein are followed by two perpendicular alpha-helices and a short beta-sheet near the N-terminus. Apolar residues in both helices form a hydrophobic core. Binding models of RAR DBD to its inverted and direct repeat response elements have been constructed based on this three-dimensional structure.
[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 study of the binding of all-trans-retinoic acid to type II human cellular retinoi
NMR study of the binding of all-trans-retinoic acid to type II human cellular retinoic acid binding protein.
Related Articles NMR study of the binding of all-trans-retinoic acid to type II human cellular retinoic acid binding protein.
Biochim Biophys Acta. 1999 Aug 17;1433(1-2):240-52
Authors: Wang L, Yan H
Cellular RA binding proteins are thought to play important roles in the (RA), a hormonally active metabolite of vitamin A that has profound effects on cell growth, + differentiation and morphogenesis. Binding of RA to type II human cellular...
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[NMR paper] NMR solution structure of type II human cellular retinoic acid binding protein: impli
NMR solution structure of type II human cellular retinoic acid binding protein: implications for ligand binding.
Related Articles NMR solution structure of type II human cellular retinoic acid binding protein: implications for ligand binding.
Biochemistry. 1998 Sep 15;37(37):12727-36
Authors: Wang L, Li Y, Abildgaard F, Markley JL, Yan H
The structure of human apo-cellular retinoic acid binding protein II (apo-CRABPII) in solution at pH 7.3 has been determined by NMR spectroscopy. The sequential assignments of the 1H, 13C, and 15N resonances...
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NMR structure of the human Mediator MED25 ACID domain.
NMR structure of the human Mediator MED25 ACID domain.
Related Articles NMR structure of the human Mediator MED25 ACID domain.
J Struct Biol. 2010 Oct 22;
Authors: Bontems F, Verger A, Dewitte F, Lens Z, Baert JL, Ferreira E, de Launoit Y, Sizun C, Guittet E, Villeret V, Monté D
MED25 (ARC92/ACID1) is a 747 residues subunit specific to higher eukaryote Mediator complex, an essential component of the RNA polymerase II general transcriptional machinery. MED25 is a target of the Herpes simplex virus transactivator protein VP16. MED25 interacts...
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[NMR paper] Structure of the Ras-binding domain of c-Raf-1 as determined by NMR spectroscopy and
Structure of the Ras-binding domain of c-Raf-1 as determined by NMR spectroscopy and identification of the region that interacts with Ras.
Related Articles Structure of the Ras-binding domain of c-Raf-1 as determined by NMR spectroscopy and identification of the region that interacts with Ras.
Drug Des Discov. 1996 Apr;13(3-4):83-93
Authors: Emerson SD, Madison VS, Palermo RE, Waugh DS, Scheffler JE, Tsao KL, Kiefer SE, Liu SP, Fry DC
The structure of the Ras-binding domain of human c-Raf-1 (residues 55 to 132) as determined in solution by NMR...
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[NMR paper] Solution structure of rat apo-S100B(beta beta) as determined by NMR spectroscopy.
Solution structure of rat apo-S100B(beta beta) as determined by NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Solution structure of rat apo-S100B(beta beta) as determined by NMR spectroscopy.
Biochemistry. 1996 Sep 10;35(36):11577-88
Authors: Drohat AC, Amburgey JC, Abildgaard F, Starich MR, Baldisseri D, Weber DJ
S100B(beta beta), a member of the S100 protein family, is a Ca(2+)-binding protein with noncovalent interactions at its dimer interface. Each apo-S100 beta...
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[NMR paper] Structure refinement of the glucocorticoid receptor-DNA binding domain from NMR data
Structure refinement of the glucocorticoid receptor-DNA binding domain from NMR data by relaxation matrix calculations.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Structure refinement of the glucocorticoid receptor-DNA binding domain from NMR data by relaxation matrix calculations.
J Mol Biol. 1995 Apr 7;247(4):689-700
Authors: van Tilborg MA, Bonvin AM, HÃ¥rd K, Davis AL, Maler B, Boelens R, Yamamoto KR, Kaptein R
The solution structure of the glucocorticoid...
The structure of the human retinoic acid receptor-beta DNA-binding domain determined
Linear Mode
