1DT7

SOLUTION STRUCTURE OF THE C-TERMINAL NEGATIVE REGULATORY DOMAIN OF P53 IN A COMPLEX WITH CA2+-BOUND S100B(BB)

Summary for 1DT7

• Entry DOI: 10.2210/pdb1dt7/pdb
• NMR Information: BMRB: 5544
• Descriptor: S100 CALCIUM-BINDING PROTEIN, CELLULAR TUMOR ANTIGEN P53, CALCIUM ION (3 entities in total)
• Functional Keywords: s100b, p53, c-terminal domain of p53, calcium-binding, ef-hand, s100 protein, four helix bundle, helix loop helix, signaling protein
• Biological source: Rattus norvegicus (Norway rat); More
• Cellular location: Cytoplasm : P04631; Cytoplasm. Isoform 1: Nucleus. Isoform 2: Nucleus. Isoform 3: Nucleus. Isoform 4: Nucleus. Isoform 7: Nucleus. Isoform 8: Nucleus. Isoform 9: Cytoplasm: P04637
• Total number of polymer chains: 4
• Total formula weight: 26868.57

Authors

Rustandi, R.R.,Baldisseri, D.M.,Weber, D.J. (deposition date: 2000-01-11, release date: 2000-07-26, Last modification date: 2024-04-10)

Primary citation

Rustandi, R.R.,Baldisseri, D.M.,Weber, D.J.
Structure of the negative regulatory domain of p53 bound to S100B(betabeta).
Nat.Struct.Biol., 7:570-574, 2000

PubMed Abstract: A Ca2+ dependent conformational change in dimeric S100B(betabeta) is required for it to bind p53 and inhibit phosphorylation of this tumor suppressor in its C-terminal negative regulatory domain. A peptide derived from this region of p53 (residues 367-388) was found to have no regular structure in its native form by NMR spectroscopy, but becomes helical when bound to Ca2+ loaded S100B(betabeta). The three-dimensional structure of this complex reveals several favorable hydrophobic and electrostatic interactions between S100B(betabeta) and the p53 peptide in the binding pocket, where S100B(betabeta) sterically blocks sites of phosphorylation and acetylation on p53 that are important for transcription activation.

PubMed: 10876243
DOI: 10.1038/76797

Experimental method

SOLUTION NMR