Fungal Transcription Factor Database
Detalied information of reference
Pubmed ID (PMID)
9630226
Paper type
Title
Crystal structure of a tyrosine phosphorylated STAT-1 dimer bound to DNA.
Abstract
The crystal structure of the DNA complex of a STAT-1 homodimer has been determined at 2.9 A resolution. STAT-1 utilizes a DNA-binding domain with an immunoglobulin fold, similar to that of NFkappaB and the p53 tumor suppressor protein. The STAT-1 dimer forms a contiguous C-shaped clamp around DNA that is stabilized by reciprocal and highly specific interactions between the SH2 domain of one monomer and the C-terminal segment, phosphorylated on tyrosine, of the other. The phosphotyrosine-binding site of the SH2 domain in each monomer is coupled structurally to the DNA-binding domain, suggesting a potential role for the SH2-phosphotyrosine interaction in the stabilization of DNA interacting elements.
Authors
Chen X, Vinkemeier U, Zhao Y, Jeruzalmi D, Darnell JE Jr, Kuriyan J.
Affiliation
The Rockefeller University, New York, New York 10021, USA.
Journal / Pages
Cell., 1998 : 93(5), 827~839