| Modification Notes |
The Oligonucleotide/oligosaccharide-binding (OB) domain is a dense structural motif normally used for nucleic acid recognition. Proteins containing an OB motif are structurally characterized by a small beta-barrel fold formed from several strands connected by modulating loops that recognize either single-stranded or unusually structured nucleic acids. The OB-fold core is extremely variable in length and in functional detail, and members of the OB-fold domain family have a low degree of sequence similarity. However, certain features of ligand binding are conserved among OB-fold complexes. OB-fold proteins are critical for DNA replication, DNA recombination, DNA repair, transcription, translation, cold shock response and telomere maintenance. OBFC1 (oligonucleotide/oligosaccharide-binding fold containing 1) is a 368 amino acid protein that may bind nucleic acids or oligosaccharides. Two isoforms of OBFC1 may exist due to alternative splicing. |