Open AccessCrystallization of hepatocyte nuclear factor 1β in complex with DNA
Author(s) -
Lu Peng,
Li Yun,
Gorman Amanda,
Chi YoungIn
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106015168
Subject(s) - dimer , crystallization , hepatocyte nuclear factors , dna , crystallography , chemistry , molecular replacement , hepatocyte , molecule , transcription factor , biophysics , biochemistry , biology , crystal structure , gene , organic chemistry , in vitro
Hepatocyte nuclear factor 1β (HNF1β) is a member of the POU transcription‐factor family and binds the target DNA as a dimer with nanomolar affinity. The HNF1β–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 Å (93.9% completeness) using a synchrotron‐radiation source under cryogenic (100 K) conditions and belong to space group R 3, with unit‐cell parameters a = b = 172.69, c = 72.43 Å. 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 HNF1β and the molecular basis of the disease‐causing mutations found in it.