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Crystallographic structure of the tetratricopeptide repeat domain of Plasmodium falciparum FKBP35 and its molecular interaction with Hsp90 C-terminal pentapeptide

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Crystallographic structure of the tetratricopeptide repeat domain of Plasmodium falciparum FKBP35 and its molecular interaction with Hsp90 C-terminal pentapeptide

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dc.contributor.author Alag, Reema
dc.contributor.author Bharatham, Nagakumar
dc.contributor.author Dong, Aiping
dc.contributor.author Hills, Tanya
dc.contributor.author Harikishore, Amaravadhi
dc.contributor.author Widjaja, Anissa Anindya
dc.contributor.author Shochat, Susana Geifman
dc.contributor.author Hui, Raymond
dc.contributor.author Yoon, Ho Sup
dc.date.accessioned 2012-10-05T04:14:21Z
dc.date.available 2012-10-05T04:14:21Z
dc.date.copyright 2009
dc.date.issued 2012-10-05
dc.identifier.citation Alag, 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.
dc.identifier.uri http://hdl.handle.net/10220/8710
dc.description.abstract Plasmodium 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.
dc.language.iso en
dc.relation.ispartofseries Protein science
dc.rights © 2009 The Protein Society
dc.subject DRNTU::Science::Chemistry::Analytical chemistry::Proteins
dc.title Crystallographic structure of the tetratricopeptide repeat domain of Plasmodium falciparum FKBP35 and its molecular interaction with Hsp90 C-terminal pentapeptide
dc.type Journal Article
dc.contributor.school School of Biological Sciences
dc.identifier.doi http://dx.doi.org/10.1002/pro.226

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