Structural highlights
Function
FKB35_PLAF7 Has peptidylprolyl isomerase (PPIase) and co-chaperone activities (PubMed:15664653, PubMed:15850699). Assists protein folding by catalyzing the peptidyl conversion of cis and trans rotamers of the prolyl amide bond of protein substrates (PubMed:15664653, PubMed:15850699, PubMed:23974147). Inhibits calcineurin phosphatase activity in vitro (PubMed:15850699, PubMed:17289400, PubMed:23974147). Plays an essential role in merozoite egress from host erythrocytes (PubMed:15664653, PubMed:23974147).[1] [2] [3] [4]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
- ↑ Monaghan P, Bell A. A Plasmodium falciparum FK506-binding protein (FKBP) with peptidyl-prolyl cis-trans isomerase and chaperone activities. Mol Biochem Parasitol. 2005 Feb;139(2):185-95. doi:, 10.1016/j.molbiopara.2004.10.007. PMID:15664653 doi:http://dx.doi.org/10.1016/j.molbiopara.2004.10.007
- ↑ Kumar R, Adams B, Musiyenko A, Shulyayeva O, Barik S. The FK506-binding protein of the malaria parasite, Plasmodium falciparum, is a FK506-sensitive chaperone with FK506-independent calcineurin-inhibitory activity. Mol Biochem Parasitol. 2005 Jun;141(2):163-73. doi:, 10.1016/j.molbiopara.2005.02.007. Epub 2005 Mar 19. PMID:15850699 doi:http://dx.doi.org/10.1016/j.molbiopara.2005.02.007
- ↑ Yoon HR, Kang CB, Chia J, Tang K, Yoon HS. Expression, purification, and molecular characterization of Plasmodium falciparum FK506-binding protein 35 (PfFKBP35). Protein Expr Purif. 2007 May;53(1):179-85. doi: 10.1016/j.pep.2006.12.019. Epub, 2006 Dec 30. PMID:17289400 doi:http://dx.doi.org/10.1016/j.pep.2006.12.019
- ↑ Harikishore A, Niang M, Rajan S, Preiser PR, Yoon HS. Small molecule Plasmodium FKBP35 inhibitor as a potential antimalaria agent. Sci Rep. 2013 Aug 26;3:2501. doi: 10.1038/srep02501. PMID:23974147 doi:10.1038/srep02501
