1DD1

CRYSTAL STRUCTURE ANALYSIS OF THE SMAD4 ACTIVE FRAGMENT

Summary for 1DD1

• Entry DOI: 10.2210/pdb1dd1/pdb
• Descriptor: SMAD4, SULFATE ION (3 entities in total)
• Functional Keywords: b-sheet sandwich helix-turn-helix, signaling protein
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: Q13485
• Total number of polymer chains: 3
• Total formula weight: 89119.90

Authors

Qin, B.Y.,Lam, S.W.,Lin, K. (deposition date: 1999-11-05, release date: 1999-11-27, Last modification date: 2024-02-07)

Primary citation

Qin, B.,Lam, S.S.,Lin, K.
Crystal structure of a transcriptionally active Smad4 fragment.
Structure Fold.Des., 7:1493-1503, 1999

PubMed Abstract: Smad4 functions as a common mediator of transforming growth factor beta (TGF-beta) signaling by forming complexes with the phosphorylated state of pathway-restricted SMAD proteins that act in specific signaling pathways to activate transcription. SMAD proteins comprise two domains, the MH1 and MH2 domain, separated by a linker region. The transcriptional activity and synergistic effect of Smad4 require a stretch of proline-rich sequence, the SMAD-activation domain (SAD), located N-terminal of the MH2 domain. To understand how the SAD contributes to Smad4 function, the crystal structure of a fragment including the SAD and MH2 domain (S4AF) was determined.

PubMed: 10647180
DOI: 10.1016/S0969-2126(00)88340-9

Experimental method

X-RAY DIFFRACTION (2.62 Å)