Crystallization and Structure Determination of the Human Estrogen Receptor by X-Ray Diffraction

摘要

The project is a postdoctoral training fellowship for Dr. Robert Nolte, tosupport X-ray crystallographic studies of cancer-related macromolecular complexes. The crystal structure of the six NH2-terminal zinc fingers of Xenopus laevis transcription factor IIIA (TFIIIA) bound with 31 base-pairs of the 5S rRNA gene promoter has been determined at 3.1 A resolution. Individual zinc fingers are positioned differently in the major groove and across the minor groove of DNA to span the entire length of the duplex. These results show how TFIIIA can recognize several separated DNA sequences using fewer fingers than necessary for continuous winding in the major groove. This structure reveals significant aspects of DNA recognition by Zn-finger proteins, which regulate many loci important for cell growth.