1TUP

TUMOR SUPPRESSOR P53 COMPLEXED WITH DNA

The structure of the DNA-binding core domain consists of a central immunoglobulin-like β-sandwich and additional structural elements that form the DNA-binding surface , which include a loop-sheet-helix motif and two large loops (L2 and L3). The architecture of the L2/L3 region is stabilized by a zinc ion, which is tetrahedrally coordinated by Cys176, His179, Cys238, and Cys242.

The DNA-binding surface, for example, overlaps with the binding sites for the carboxy-terminal domain of ASPP2 , the BRCT region of 53BP1 , and the large T-antigen of SV40 , with significant conformational variability of the L3 loop region (residues 240–250) in the various interfaces .
Authors
Cho, Y.Gorina, S.Jeffrey, P.D.Pavletich, N.P.
Title

Crystal structure of a p53 tumor suppressor-DNA complex: understanding tumorigenic mutations.


Journal (PubMed)

PDB ID (PDB)

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