ridm@nrct.go.th   ระบบคลังข้อมูลงานวิจัยไทย   รายการโปรดที่คุณเลือกไว้

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

หน่วยงาน Nanyang Technological University, Singapore

รายละเอียด

ชื่อเรื่อง : Crystallographic structure of the tetratricopeptide repeat domain of Plasmodium falciparum FKBP35 and its molecular interaction with Hsp90 C-terminal pentapeptide
นักวิจัย : Alag, Reema , Bharatham, Nagakumar , Dong, Aiping , Hills, Tanya , Harikishore, Amaravadhi , Widjaja, Anissa Anindya , Shochat, Susana Geifman , Hui, Raymond , Yoon, Ho Sup
คำค้น : DRNTU::Science::Chemistry::Analytical chemistry::Proteins
หน่วยงาน : Nanyang Technological University, Singapore
ผู้ร่วมงาน : -
ปีพิมพ์ : 2552
อ้างอิง : 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. , http://hdl.handle.net/10220/8710 , http://dx.doi.org/10.1002/pro.226
ที่มา : -
ความเชี่ยวชาญ : -
ความสัมพันธ์ : Protein science
ขอบเขตของเนื้อหา : -
บทคัดย่อ/คำอธิบาย :

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.

บรรณานุกรม :
Alag, Reema , Bharatham, Nagakumar , Dong, Aiping , Hills, Tanya , Harikishore, Amaravadhi , Widjaja, Anissa Anindya , Shochat, Susana Geifman , Hui, Raymond , Yoon, Ho Sup . (2552). Crystallographic structure of the tetratricopeptide repeat domain of Plasmodium falciparum FKBP35 and its molecular interaction with Hsp90 C-terminal pentapeptide.
    กรุงเทพมหานคร : Nanyang Technological University, Singapore.
Alag, Reema , Bharatham, Nagakumar , Dong, Aiping , Hills, Tanya , Harikishore, Amaravadhi , Widjaja, Anissa Anindya , Shochat, Susana Geifman , Hui, Raymond , Yoon, Ho Sup . 2552. "Crystallographic structure of the tetratricopeptide repeat domain of Plasmodium falciparum FKBP35 and its molecular interaction with Hsp90 C-terminal pentapeptide".
    กรุงเทพมหานคร : Nanyang Technological University, Singapore.
Alag, Reema , Bharatham, Nagakumar , Dong, Aiping , Hills, Tanya , Harikishore, Amaravadhi , Widjaja, Anissa Anindya , Shochat, Susana Geifman , Hui, Raymond , Yoon, Ho Sup . "Crystallographic structure of the tetratricopeptide repeat domain of Plasmodium falciparum FKBP35 and its molecular interaction with Hsp90 C-terminal pentapeptide."
    กรุงเทพมหานคร : Nanyang Technological University, Singapore, 2552. Print.
Alag, Reema , Bharatham, Nagakumar , Dong, Aiping , Hills, Tanya , Harikishore, Amaravadhi , Widjaja, Anissa Anindya , Shochat, Susana Geifman , Hui, Raymond , Yoon, Ho Sup . Crystallographic structure of the tetratricopeptide repeat domain of Plasmodium falciparum FKBP35 and its molecular interaction with Hsp90 C-terminal pentapeptide. กรุงเทพมหานคร : Nanyang Technological University, Singapore; 2552.