Seroatlas · Protein domains

Nucleic acid-binding, OB-fold

IPR012340

Definition

A five-stranded β-barrel was first noted as a common structure among four proteins binding single-stranded nucleic acids (staphylococcal nuclease and aspartyl-tRNA synthetase) or oligosaccharides (B subunits of enterotoxin and verotoxin-1), and has been termed the oligonucleotide/oligosaccharide binding motif, or OB fold, a five-stranded β-sheet coiled to form a closed β-barrel capped by an α helix located between the third and fourth strands PMID:12769718. Two ribosomal proteins, S17 and S1, are members of this class and have different variations of the OB fold theme. Comparisons with other OB fold nucleic acid binding proteins suggest somewhat different mechanisms of nucleic acid recognition in each case PMID:9862955. There are many nucleic acid-binding proteins that contain domains with this OB-fold structure, including: Large ribosomal subunit protein uL2 Small ribosomal subunit protein uS12 DNA ligase Polyribonucleotide nucleotidyltransferase Phage ssDNA-binding proteins (gp32, gp2.5, gpV) Holliday junction branch migration complex subunit RuvA Elongation factor P

87 human proteins with this domain

Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.

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