2gda
From Proteopedia
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REFINED SOLUTION STRUCTURE OF THE GLUCOCORTICOID RECEPTOR DNA-BINDING DOMAIN
Overview
A refined solution structure of the glucocorticoid receptor DNA-binding, domain (GR DBD) has been determined using two- and three-dimensional, nuclear magnetic resonance (NMR) spectroscopy on an 15N-labeled GR DBD, fragment in conjunction with distance geometry and simulated annealing, calculations. Thirty structures of the fragment C440-R510 of the rat GR, were calculated based on 906 distance constraints obtained from NOE, intensities (168 intraresidue and 738 interresidue NOEs) and 43 dihedral, constraints. Average atomic root mean square (rms) differences between the, 24 best structures and their geometric average are 0.70 A for backbone, atoms and 1.44 A for all heavy atoms. Several regions that were not well, defined in a previous NMR structure determination of a similar protein, fragment [Hard, T., Kellenbach, E., Boelens, R., Maler, B.A., Dahlman, K., Freedman, L.P., Carlstedt-Duke, J., Yamamoto, K.R., Gustafsson, J.-A., &, Kaptein, R. (1990b) Science 249, 157-160] are now well-defined. The, refined structure of the uncomplexed GR DBD is very similar to the crystal, structure of GR DBD in a sequence specific DNA complex [Luisi, B. F., Xu, W. X., Otwinowski, Z., Freeman, L. P., Yamamoto, K. R., & Sigler, P. B., (1991) Nature 352, 497-505], in particular with regard to the presence and, relative positions of secondary structure elements. The backbone atom rms, difference between the average NMR solution structure and the crystal, structure of the DNA-complexed GR DBD is 1.8 A. The most pronounced, differences between the free and DNA-complexed states are found within the, fragment C476-C482 in the second zinc-coordinating domain.(ABSTRACT, TRUNCATED AT 250 WORDS)
About this Structure
2GDA is a Single protein structure of sequence from Rattus norvegicus with ZN as ligand. Full crystallographic information is available from OCA.
Reference
Refined solution structure of the glucocorticoid receptor DNA-binding domain., Baumann H, Paulsen K, Kovacs H, Berglund H, Wright AP, Gustafsson JA, Hard T, Biochemistry. 1993 Dec 14;32(49):13463-71. PMID:8257681
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