Biology:KAHRP
| Knob-associated histidine-rich protein | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Organism | |||||||
| Symbol | ? | ||||||
| UniProt | P09346 | ||||||
| |||||||
| EMP3-KAHRP-like N-terminal domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | EKAL | ||||||||
| Pfam | PF17986 | ||||||||
| InterPro | IPR040805 | ||||||||
| |||||||||
| EMP3 refers to "Erythrocyte membrane protein 3." It is likely a misnomer, as no reported PfEMP3 sequences contain this domain. PfEMP3 is arranged next to KAHRP in the P. falciparum genome, a probable cause of misidentification. | |||||||||
KAHRP (knob-associated histidine-rich protein) is a protein expressed by Plasmodium falciparum infecting erythrocytes. KAHRP is a major component of knobs, feature found on Plasmodium falciparum infected erythrocytes.
It has been suggested that KAHRP may play a role in trafficking or docking PfEMP1, major malarial cytoadherence protein to the erythrocyte membrane;[1] however, these findings were disputed by recent NMR and fluorescence anisotropy studies showing no interaction between PfEMP1 and KAHRP.[2]
Instead, KAHRP was shown to interact with Ankyrin, more precisely the D3 subunit of the Membrane-binding domain of Ankyrin type 1.[3] This interaction was suggested via SPR, ELISA, and Pulldown studies, however, it has not been confirmed by NMR, ITC, crystallography, or fluorescence anisotropy.[citation needed]
References
- ↑ "Malaria parasite proteins that remodel the host erythrocyte". Nature Reviews. Microbiology 7 (5): 341–54. May 2009. doi:10.1038/nrmicro2110. PMID 19369950.
- ↑ "Structural analysis of the Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) intracellular domain reveals a conserved interaction epitope". The Journal of Biological Chemistry 287 (10): 7182–9. March 2012. doi:10.1074/jbc.M111.330779. PMID 22249178.
- ↑ "Interaction of Plasmodium falciparum knob-associated histidine-rich protein (KAHRP) with erythrocyte ankyrin R is required for its attachment to the erythrocyte membrane". Biochimica et Biophysica Acta (BBA) - Biomembranes 1838 (1 Pt B): 185–92. January 2014. doi:10.1016/j.bbamem.2013.09.014. PMID 24090929.
 |  |
