BNR/Asp-box repeat

Available protein structures:
PDB	IPR002860 PF02012 (ECOD; PDBsum)
AlphaFold	IPR002860; PF02012;

BNR/Asp-box repeat
BNR/Asp-box repeat
	Structure of a bacterial sialidase.
Identifiers
Symbol	BNR
Pfam	PF02012
Pfam clan	CL0434
InterPro	IPR002860
SCOP2	1euu / SCOPe / SUPFAM
PDB
Available protein structures:
PDB	IPR002860 PF02012 (ECOD; PDBsum)
AlphaFold	IPR002860; PF02012;

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.²³ 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:

NEU1
NEU2
NEU3
RELN
SORCS1
SORCS2
SORCS3
SORL1
SORT1

References

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.
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.
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.
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

[pmid8591030-1] 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.

[PUB00014861-4] 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.

1

2

3

4