Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/95073
Title: Crystallographic structure of the tetratricopeptide repeat domain of Plasmodium falciparum FKBP35 and its molecular interaction with Hsp90 C-terminal pentapeptide
Authors: Alag, Reema
Bharatham, Nagakumar
Dong, Aiping
Hills, Tanya
Harikishore, Amaravadhi
Widjaja, Anissa Anindya
Shochat, Susana Geifman
Hui, Raymond
Yoon, Ho Sup
Keywords: DRNTU::Science::Chemistry::Analytical chemistry::Proteins
Issue Date: 2009
Source: 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.
Series/Report no.: Protein science
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.
URI: https://hdl.handle.net/10356/95073
http://hdl.handle.net/10220/8710
DOI: 10.1002/pro.226
Rights: © 2009 The Protein Society
Fulltext Permission: none
Fulltext Availability: No Fulltext
Appears in Collections:SBS Journal Articles

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