BNR/Asp-box repeat
Structure of a bacterial sialidase.[1]
Identifiers
SymbolBNR
PfamPF02012
Pfam clanCL0434
InterProIPR002860
SCOP21euu / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

BNR/Asp-box repeat is a repetitive sequence of amino acids contained in some proteins. Many of these proteins contain multiple BNR (bacterial neuraminidase repeat) repeats or Asp-boxes.

The repeats are short, however the repeats are never found closer than 40 residues together suggesting that the repeat is structurally longer. The Asp-box itself adopts a well-defined beta-hairpin fold.[2][3] These repeats are found in a variety of non-homologous proteins, including bacterial ribonucleases, sulphite oxidases, reelin, netrins, sialidases, neuraminidases, some lipoprotein receptors, and a variety of glycosyl hydrolases.[4]

Examples

Human genes encoding proteins containing this domain include:

References

  1. Gaskell A, Crennell S, Taylor G (November 1995). "The three domains of a bacterial sialidase: a beta-propeller, an immunoglobulin module and a galactose-binding jelly-roll". Structure. 3 (11): 1197–1205. doi:10.1016/s0969-2126(01)00255-6. PMID 8591030.
  2. Crennell SJ, Garman EF, Laver WG, Vimr ER, Taylor GL (November 1993). "Crystal structure of a bacterial sialidase (from Salmonella typhimurium LT2) shows the same fold as an influenza virus neuraminidase". Proceedings of the National Academy of Sciences of the United States of America. 90 (21): 9852–9856. Bibcode:1993PNAS...90.9852C. doi:10.1073/pnas.90.21.9852. PMC 47670. PMID 8234325.
  3. Quistgaard EM, Thirup SS (July 2009). "Sequence and structural analysis of the Asp-box motif and Asp-box beta-propellers; a widespread propeller-type characteristic of the Vps10 domain family and several glycoside hydrolase families". BMC Structural Biology. 9: 46. doi:10.1186/1472-6807-9-46. PMC 2716378. PMID 19594936.
  4. Copley RR, Russell RB, Ponting CP (February 2001). "Sialidase-like Asp-boxes: sequence-similar structures within different protein folds". Protein Science. 10 (2): 285–292. doi:10.1110/ps.31901. PMC 2373934. PMID 11266614.
This article incorporates text from the public domain Pfam and InterPro: IPR002860
This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.