dc.contributor.authorAlag, Reema
dc.contributor.authorBharatham, Nagakumar
dc.contributor.authorDong, Aiping
dc.contributor.authorHills, Tanya
dc.contributor.authorHarikishore, Amaravadhi
dc.contributor.authorWidjaja, Anissa Anindya
dc.contributor.authorShochat, Susana Geifman
dc.contributor.authorHui, Raymond
dc.contributor.authorYoon, Ho Sup
dc.date.accessioned2012-10-05T04:14:21Z
dc.date.available2012-10-05T04:14:21Z
dc.date.copyright2009en_US
dc.date.issued2009
dc.identifier.citationAlag, R., Bharatham, N., Dong, A., Hills, T., Harikishore, A., Widjaja, A. A., et al. (2009). Crystallographic structure of the tetratricopeptide repeat domain of Plasmodium falciparum FKBP35 and its molecular interaction with Hsp90 C-terminal pentapeptide. Protein Science, 18(10), 2115-2124.en_US
dc.identifier.urihttp://hdl.handle.net/10220/8710
dc.description.abstractPlasmodium falciparum FK506-binding protein 35 (PfFKBP35) that binds to FK506 contains a conserved tetratricopeptide repeat (TPR) domain. Several known TPR domains such as Hop, PPP5, CHIP, and FKBP52 are structurally conserved and are able to interact with molecular chaperones such as Hsp70/Hsp90. Here, we present the crystal structure of PfFKBP35-TPR and demonstrate its interaction with Hsp90 C-terminal pentapeptide (MEEVD) by surface plasmon resonance and nuclear magnetic resonance spectroscopy-based binding studies. Our sequence and structural analyses reveal that PfFKBP35 is similar to Hop and PPP5 in possessing all the conserved residues which are important for carboxylate clamping with Hsp90. Mutational studies were carried out on positively charged clamp residues that are crucial for binding to carboxylate groups of aspartate, showing that all the mutated residues are important for Hsp90 binding. Molecular docking and electrostatic calculations demonstrated that the MEEVD peptide of Hsp90 can form aspartate clamp unlike FKBP52. Our results provide insightful information and structural basis about the molecular interaction between PfFKBP35-TPR and Hsp90.en_US
dc.language.isoenen_US
dc.relation.ispartofseriesProtein scienceen_US
dc.rights© 2009 The Protein Societyen_US
dc.subjectDRNTU::Science::Chemistry::Analytical chemistry::Proteins
dc.titleCrystallographic structure of the tetratricopeptide repeat domain of Plasmodium falciparum FKBP35 and its molecular interaction with Hsp90 C-terminal pentapeptideen_US
dc.typeJournal Article
dc.contributor.schoolSchool of Biological Sciencesen_US
dc.identifier.doihttp://dx.doi.org/10.1002/pro.226


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