Crystallization of hepatocyte nuclear factor 1beta in complex with DNA. Acta Crystallogr Sect F Struct Biol Cryst Commun 2006 Jun 01;62(Pt 6):525-9
Date
06/07/2006Pubmed ID
16754972Pubmed Central ID
PMC1581457DOI
10.1107/S1744309106015168Scopus ID
2-s2.0-33745168228 (requires institutional sign-in at Scopus site) 5 CitationsAbstract
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.
Author List
Lu P, Li Y, Gorman A, Chi YIAuthor
Young-In Chi PhD Assistant Professor in the Surgery department at Medical College of WisconsinMESH terms used to index this publication - Major topics in bold
CrystallizationDNA
Hepatocyte Nuclear Factor 1-beta
Protein Binding
Solvents
X-Ray Diffraction
