The structure of the human retinoic acid receptor-beta DNA-binding domain determined by NMR.
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.
Katahira
M
M
University of Utrecht, The Netherlands.
Knegtel
R
R
Schilthius
J
J
Boelens
R
R
Eib
D
D
van der Saag
P
P
Kaptein
R
R
D002352:Carrier Proteins / Q000737:chemistry* / Q000378:metabolism; D004247:DNA / Q000737:chemistry*; D004268:DNA-Binding Proteins / Q000737:chemistry*; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation; D018168:Receptors, Retinoic Acid; D014212:Tretinoin / Q000378:metabolism*
D002352:Carrier Proteins; D004268:DNA-Binding Proteins; D018168:Receptors, Retinoic Acid; D014212:Tretinoin; D004247:DNA