1MHD

CRYSTAL STRUCTURE OF A SMAD MH1 DOMAIN BOUND TO DNA

Summary for 1MHD

• Entry DOI: 10.2210/pdb1mhd/pdb
• Descriptor: DNA, SMAD3, ... (4 entities in total)
• Functional Keywords: complex (transcription activator-dna), smad3 mh1, smad binding element, dna, complex (transcription activator-dna) complex, complex (transcription activator/dna)
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: P84022
• Total number of polymer chains: 4
• Total formula weight: 39332.76

Authors

Shi, Y. (deposition date: 1998-08-18, release date: 1999-08-18, Last modification date: 2024-10-23)

Primary citation

Shi, Y.,Wang, Y.F.,Jayaraman, L.,Yang, H.,Massague, J.,Pavletich, N.P.
Crystal structure of a Smad MH1 domain bound to DNA: insights on DNA binding in TGF-beta signaling.
Cell(Cambridge,Mass.), 94:585-594, 1998

PubMed Abstract: The Smad family of proteins, which are frequently targeted by tumorigenic mutations in cancer, mediate TGF-beta signaling from cell membrane to nucleus. The crystal structure of a Smad3 MH1 domain bound to an optimal DNA sequence determined at 2.8 A resolution reveals a novel DNA-binding motif. In the crystals, base-specific DNA recognition is provided exclusively by a conserved 11-residue beta hairpin that is embedded in the major groove of DNA. A surface loop region, to which tumorigenic mutations map, has been identified as a functional surface important for Smad activity. This structure establishes a framework for understanding how Smad proteins may act in concert with other transcription factors in the regulation of TGF-beta-responsive genes.

PubMed: 9741623
DOI: 10.1016/S0092-8674(00)81600-1

Experimental method

X-RAY DIFFRACTION (2.8 Å)