Crystal structure of an OCA-B peptide bound to an Oct-1 POU domain/octamer DNA complex: specific recognition of a protein-DNA interface

Article Abstract:

An OCA-B peptide bound to an Oct-1 POU domain/octamer DNA complex is discussed relative to crystal structure and specific recognition of a protein-DNA interface. The structure of a ternary complex has been established to help in understanding of the structural basis for combinatorial control and sequence-specific recognition in regulation of immunoglobulin gene expression. The OCA-B peptide binds in the major groove near the center of the octamer site. Its polypeptide backbone sets up a pair of hydrogen bonds with the adenine base at position 5 of the octamer DNA.

United States, Statistical Data Included, Research, Analysis, Physiological aspects, DNA, Gene expression, Genetic transcription, Transcription (Genetics), Immunocytochemistry, Crystals, Crystal structure, DNA binding proteins, Hydrogen bonding, Hydrogen bonds

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Classification of introns: U2-type or U12-type

Article Abstract:

Dinucleotides GT and AG were recognized with the first intron sequencing, and it was suggested that dinucleotides were almost universal, of a common origin. Later exceptions identified a sub-class with AT and AC at the 5' and 3' boundaries on introns. Examples of intron subsets with boundary sequences AT-AC, possibly spliced by the U12 system, are provided. Further study of U12 spliceosomes may suggest the origin of the parts of both types of spliceosomes and their link to group II-type self-splicing introns.

Observations, Nucleotides, Introns

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