Basis for recognition of cisplatin-modified DNA by high-mobility-group proteins

Article Abstract:

It has been possible to determine the structure of a 1:1 cisplatin-modified DNA/high-mobility-group (HMG)-domain complex. It was established that the HMG domain binds with its concave surface contacting the minor groove of the DNA duplex. A sharp bend is found at the site of the cisplatin-induced DNA crosslink, but the link between this bend and the protein-binding site is different from that in the structures of sequence-specific HMG domains. Information about how structure-specific HMG-domain proteins bind to cisplatin-modified DNA should offer a basis for the design of new chemotherapeutic strategies.

Protein binding, DNA binding proteins

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Crystal structure of double-stranded DNA containing the major adduct of the anticancer drug cisplatin

Article Abstract:

An analysis of the X-ray structure of the double stranded dodecamer formed by the binding of cis-(Pt(NH3)2(d(pGpG))) to DNA shows that cisplatin binds to N7 which causes bending of the molecule in the G6 and G7 guanoside amino acids area. The addition of the d(GpG) to DNA duplex distorts the platinum coordination geometry and increases the energy of the complex. This extra energy is released when high-mobility-group (HMG) molecules bind to the DNA. The binding of d(GpG) and d(ApG) cisplatin adducts to DNA enables structural changes in the DNA to allow its binding to HMG containing proteins.

Observations, Molecular structure, DNA-ligand interactions, DNA binding, Cisplatin

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Frank Albert Cotton (1930-2007)

Article Abstract:

Frank Albert Cotton, an Inorganic chemist, educator and discoverer of the quadruple bond was a champion of fundamental research. He championed the cause of funding basic research that is driven purely by intellectual curiosity.

United States, Obituary, Inorganic chemists, Cotton, Frank Albert

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