Crystal structure of p50/p65 heterodimer of transcription factor NF-kappa-B bound to DNA

Article Abstract:

It has been possible to identify the crystal structure of the p50/p65 heterodimer bound to the kappa-B DNA of the intronic enhancer of the immunoglobulin light-chain gene. There is a 5-base-pair 5' subsite for p50, with a 4-base-pair 3' subsite for p65. The p50/p65 heterodimer has a very high DNA affinity compared with most eukaryotic transcription factors. A number of sources could contribute to this high binding affinity, including interdomain interactions in both subunits providing a high level of cooperativity between the two DNA-contacting domains.

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DNA binding by the ETS domain

Article Abstract:

Eukaryotic transcription factors bind specific DNA sequences through the 85-residue ETS domain. Analyses of the ETS-domain-DNA interactions reveal that the ETS domain comprises of three helices and a four-stranded antiparallel beta-sheet. This composition makes the ETS-domain proteins members of the winged helix-turn-helix structural family. The helix-turn-helix recognizes the 5'-GGAA-3' sequence in the DNA and results in binding.

Analysis, DNA binding proteins

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Crystal structure of the GreA transcript cleavage factor from Escherichia coli

Article Abstract:

Stereoimaging helps study the crystal structure of GreA, a transcription elongation factor from Escherichia coli, which has en extended amino-terminal domain. Charge distribution in the crystal is asymmetrical and the extended structure is a coiled-coil antiparallel alpha-helical dimer. The tip of the dimer interacts with the 3'-end of the transcript, participating in the transcript cleavage reaction.

Proteins, Protein structure

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