OB-fold

Oligonucleotide/oligosaccharide binding fold
Cartoon representation of the crystal structure of human mitochondrial single-stranded DNA binding protein (PDB: 3ull​) [1]
Identifiers
SymbolOB-fold
Pfam clanCL0021
ECOD2
InterProIPR012340

In molecular biology, the OB-fold (oligonucleotide/oligosaccharide-binding fold) is a small protein structural motif observed in different proteins that bind oligonucleotides or oligosaccharides. It was originally identified in 1993 in four unrelated proteins: staphylococcal nuclease, anticodon binding domain of aspartyl-tRNA synthetase, and the B-subunits of heat-labile enterotoxin and verotoxin-1.[2] Since then it has been found in multiple proteins many of which are involved in genome stability.[3][4] This fold is often described as a Greek key motif.[2][5]

  1. ^ Yang C, Curth U, Urbanke C, Kang C (February 1997). "Crystal structure of human mitochondrial single-stranded DNA binding protein at 2.4 A resolution". Nature Structural Biology. 4 (2): 153–157. doi:10.1038/nsb0297-153. PMID 9033597.
  2. ^ a b Cite error: The named reference Murzin_1993 was invoked but never defined (see the help page).
  3. ^ Amir M, Alam A, Ishrat R, Alajmi MF, Hussain A, Rehman MT, et al. (September 2020). "A Systems View of the Genome Guardians: Mapping the Signaling Circuitry Underlying Oligonucleotide/Oligosaccharide-Binding Fold Proteins". Omics. 24 (9): 518–530. doi:10.1089/omi.2020.0072. PMID 32780668.
  4. ^ Yang Z, Costanzo M, Golde DW, Kolesnick RN (September 1993). "Tumor necrosis factor activation of the sphingomyelin pathway signals nuclear factor kappa B translocation in intact HL-60 cells". The Journal of Biological Chemistry. 268 (27): 20520–20523. doi:10.1016/s0021-9258(20)80756-x. PMC 8376408. PMID 8376408.
  5. ^ Cite error: The named reference Theobald_2003 was invoked but never defined (see the help page).