Accession Number : ADA319775

Title :   Structural Studies of the PU.1 Transcription Factor.

Descriptive Note : Annual rept. 1 Sep 95-31 Aug 96,

Corporate Author : BURNHAM INST LA JOLLA CA

Personal Author(s) : Ely, Kathryn R.

PDF Url : ADA319775

Report Date : OCT 1996

Pagination or Media Count : 30

Abstract : Ets transcription factors play a role in development and are implicated in some malignant processes. Recently, members of this large gene family have been identified in normal gene expression in mammary cells and also in breast cancer cell lines. In these studies, the crystal structure of the DNA-binding domain of the PU.1 ets protein complexed to DNA has been determined at 2.3 A resolution. The DNA binding domain is a conserved region that binds the core sequence 5'-GGAA/T-3'. The PU.1 domain binds DNA using a loop-helix-loop motif involving conserved amino acids and bases. In this project we are also using nuclear magnetic resonance (NMR) to determine the unbound structure of the domain in solution. The two structures are being correlated to understand the process of DNA recognition by ets proteins.

Descriptors :   *DEOXYRIBONUCLEIC ACIDS, *MAMMARY GLANDS, *BREAST CANCER, CRYSTAL STRUCTURE, NUCLEAR MAGNETIC RESONANCE, STRUCTURAL PROPERTIES, PROTEINS, RECOGNITION, MAST CELLS, GENES, IMMUNE SERUMS, CELLS(BIOLOGY), AMINO ACIDS, METABOLIC DISEASES.

Subject Categories : Medicine and Medical Research
      Microbiology

Distribution Statement : APPROVED FOR PUBLIC RELEASE