Crystallization and preliminary X-ray analysis of Pit-1 POU domain complexed to a 28 base pair DNA element.
The POU domain, representing an approximately 150 amino acid conserved region, serves as the DNA-recognition domain for a large number of eukaryotic transcription factors. Bipartite in nature, the POU domain is comprised of a N-terminal POU-specific domain connected by a linker of variable length to a C-terminal homeodomain. We report here co-crystals of pituitary-specific factor Pit-1 POU domain bound as a dimer to a 28 bp DNA fragment. The crystals diffract to at least 2.3 angstroms in resolution and belong to space group P1 with unit cell dimensions of a = 42.5 angstroms, b = 50.1 angstroms, c = 55.8 angstroms, alpha = 76.7 degrees, beta = 79.3 degrees, and gamma = 67.2 degrees.
Jacobson
E M
EM
Department of Biochemistry and Molecular Biophysics, Columbia University, New York 10032, USA.
Li
P
P
Rosenfeld
M G
MG
Aggarwal
A K
AK
D001483:Base Sequence; D018360:Crystallography, X-Ray; D004247:DNA / Q000737:chemistry*; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000235:genetics; D008968:Molecular Conformation; D008969:Molecular Sequence Data; D050809:POU Domain Factors; D010446:Peptide Fragments / Q000737:chemistry* / Q000235:genetics; D011994:Recombinant Proteins / Q000737:chemistry; D012045:Regulatory Sequences, Nucleic Acid; D050817:Transcription Factor Pit-1; D014157:Transcription Factors / Q000737:chemistry* / Q000235:genetics
D004268:DNA-Binding Proteins; D050809:POU Domain Factors; D010446:Peptide Fragments; D011994:Recombinant Proteins; D050817:Transcription Factor Pit-1; D014157:Transcription Factors; D004247:DNA