InterPro : IPR017360

Name  Anthrax toxin receptor Short Name  Anthrax_toxin_rcpt
Type  Family Description  Anthrax is an acute disease in humans and animals, which is caused by the bacterium Bacillus anthracis. While the disease can be lethal, there are effective vaccines against anthrax, and some forms of the disease respond well to antibiotic treatment.The anthrax toxin consists of the proteins protective antigen (PA), lethalfactor (LF) and oedema factor (EF). The first step of toxin entry into host cells is the recognition by PA of a receptor on the surface of the target cell. The subsequent cleavage of receptor-bound PA enables EF and LF to bind and form a heptameric PA63 pre-pore, which triggers endocytosis. PA has been shown to bind to two cellular receptors, termed anthrax toxin receptor 1 and 2. Both bind to PA with high affinity and are capable of mediating toxicity [, ], and both are type 1 membrane proteins that include an approximately 200-aa extracellular von Willebrand factor A (VWA) domain with a metal ion-dependent adhesion site (MIDAS) motif [].This entry represents the anthrax toxin receptors.
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Sequence Features

GO Displayer

Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

3 Contains

Id Name Short Name Type
IPR002035 von Willebrand factor, type A VWF_A Domain
IPR008399 Anthrax toxin receptor, C-terminal Anthrax_toxin_rcpt_C Domain
IPR008400 Anthrax toxin receptor, extracellular Anthrax_toxin_rcpt_extracel Domain

0 Found In

0 Parent Features

2 Publications

First Author Title Year Journal Volume Pages
Lacy DB Crystal structure of the von Willebrand factor A domain of human capillary morphogenesis protein 2: an anthrax toxin receptor. 2004 Proc Natl Acad Sci U S A 101 6367-72
Santelli E Crystal structure of a complex between anthrax toxin and its host cell receptor. 2004 Nature 430 905-8



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)