Two structures of cyclophilin 40: folding and fidelity in the TPR domains

P Taylor; J Dornan; A Carrello; R F Minchin; T Ratajczak; M D Walkinshaw

Two structures of cyclophilin 40: folding and fidelity in the TPR domains

P Taylor, J Dornan, A Carrello, R F Minchin, T Ratajczak, M D Walkinshaw

School of Biological Sciences

Research output: Contribution to journal › Article › peer-review

Abstract / Description of output

The "large immunophilin" family consists of domains of cyclophilin or FK506 binding protein linked to a tetratricopeptide (TPR) domain. They are intimately associated with steroid receptor complexes and bind to the C-terminal domain of Hsp90 via the TPR domain. The competitive binding of specific large immunophilins and other TPR-Hsp90 proteins provides a regulatory mechanism for Hsp90 chaperone activity.

Original language	English
Pages (from-to)	431-8
Number of pages	8
Journal	Structure
Volume	9
Issue number	5
Publication status	Published - 2001

Cite this

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title = "Two structures of cyclophilin 40: folding and fidelity in the TPR domains",

abstract = "The {"}large immunophilin{"} family consists of domains of cyclophilin or FK506 binding protein linked to a tetratricopeptide (TPR) domain. They are intimately associated with steroid receptor complexes and bind to the C-terminal domain of Hsp90 via the TPR domain. The competitive binding of specific large immunophilins and other TPR-Hsp90 proteins provides a regulatory mechanism for Hsp90 chaperone activity.",

author = "P Taylor and J Dornan and A Carrello and Minchin, {R F} and T Ratajczak and Walkinshaw, {M D}",

year = "2001",

language = "English",

volume = "9",

pages = "431--8",

journal = "Structure",

issn = "0969-2126",

publisher = "Cell Press",

number = "5",

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TY - JOUR

T1 - Two structures of cyclophilin 40

T2 - folding and fidelity in the TPR domains

AU - Taylor, P

AU - Dornan, J

AU - Carrello, A

AU - Minchin, R F

AU - Ratajczak, T

AU - Walkinshaw, M D

PY - 2001

Y1 - 2001

N2 - The "large immunophilin" family consists of domains of cyclophilin or FK506 binding protein linked to a tetratricopeptide (TPR) domain. They are intimately associated with steroid receptor complexes and bind to the C-terminal domain of Hsp90 via the TPR domain. The competitive binding of specific large immunophilins and other TPR-Hsp90 proteins provides a regulatory mechanism for Hsp90 chaperone activity.

AB - The "large immunophilin" family consists of domains of cyclophilin or FK506 binding protein linked to a tetratricopeptide (TPR) domain. They are intimately associated with steroid receptor complexes and bind to the C-terminal domain of Hsp90 via the TPR domain. The competitive binding of specific large immunophilins and other TPR-Hsp90 proteins provides a regulatory mechanism for Hsp90 chaperone activity.

M3 - Article

C2 - 11377203

SN - 0969-2126

VL - 9

SP - 431

EP - 438

JO - Structure

JF - Structure

IS - 5

ER -

Two structures of cyclophilin 40: folding and fidelity in the TPR domains

Abstract / Description of output

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