Crystallization of hepatocyte nuclear factor 1beta in complex with DNA.
Hepatocyte nuclear factor 1beta (HNF1beta) is a member of the POU transcription-factor family and binds the target DNA as a dimer with nanomolar affinity. The HNF1beta-DNA complex has been prepared and crystallized by hanging-drop vapor diffusion in 6%(v/v) PEG 300, 5%(w/v) PEG 8000, 8%(v/v) glycerol and 0.1 M Tris pH 8.0. The crystals diffracted to 3.2 A (93.9% completeness) using a synchrotron-radiation source under cryogenic (100 K) conditions and belong to space group R3, with unit-cell parameters a = b = 172.69, c = 72.43 A. A molecular-replacement solution has been obtained and structure refinement is in progress. This structure will shed light on the molecular mechanism of promoter recognition by HNF1beta and the molecular basis of the disease-causing mutations found in it.
Lu
Peng
P
Department of Molecular and Cellular Biochemistry and Center for Structural Biology, University of Kentucky, Lexington, KY 40536, USA.
Li
Yun
Y
Gorman
Amanda
A
Chi
Young-In
YI
D003460:Crystallization / Q000379:methods; D004247:DNA / Q000737:chemistry* / Q000378:metabolism; D051539:Hepatocyte Nuclear Factor 1-beta / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding; D012997:Solvents; D014961:X-Ray Diffraction
D012997:Solvents; D051539:Hepatocyte Nuclear Factor 1-beta; D004247:DNA