1BF5

TYROSINE PHOSPHORYLATED STAT-1/DNA COMPLEX

Summary for 1BF5

• Entry DOI: 10.2210/pdb1bf5/pdb
• Descriptor: DNA (5'-D(*AP*CP*AP*GP*TP*TP*TP*CP*CP*CP*GP*TP*AP*AP*AP*TP*G P*C)-3'), DNA (5'-D(*TP*GP*CP*AP*TP*TP*TP*AP*CP*GP*GP*GP*AP*AP*AP*CP*T P*G)-3'), SIGNAL TRANSDUCER AND ACTIVATOR OF TRANSCRIPTION 1-ALPHA/BETA (3 entities in total)
• Functional Keywords: complex (sh2 domain-dna), sh2 domain, transcription factor, gene regulation-dna complex, gene regulation/dna
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm : P42224
• Total number of polymer chains: 3
• Total formula weight: 77688.49

Authors

Kuriyan, J.,Zhao, Y.,Chen, X.,Vinkemeier, U.,Jeruzalmi, D.,Darnell Jr., J.E. (deposition date: 1998-05-27, release date: 1998-08-12, Last modification date: 2024-11-20)

Primary citation

Chen, X.,Vinkemeier, U.,Zhao, Y.,Jeruzalmi, D.,Darnell Jr., J.E.,Kuriyan, J.
Crystal structure of a tyrosine phosphorylated STAT-1 dimer bound to DNA.
Cell(Cambridge,Mass.), 93:827-839, 1998

PubMed 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.

PubMed: 9630226
DOI: 10.1016/S0092-8674(00)81443-9

Experimental method

X-RAY DIFFRACTION (2.9 Å)