Use this URL to cite or link to this record in EThOS: http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.649656
Title: Immunophilins : an investigation into function and structure
Author: Dornan, Jacqueline
Awarding Body: University of Edinburgh
Current Institution: University of Edinburgh
Date of Award: 2001
Availability of Full Text:
Access from EThOS:
Full text unavailable from EThOS. Please try the link below.
Access from Institution:
Abstract:
The work described in this thesis focused on the over-expression, purification, biochemical characterisation, crystallisation and 3-D structure determination of three members of the immunophilin family. The overall goal of the project was to use biochemical and structural information derived from these studies to assist in the elucidation of the various roles played by these proteins in diverse systems. Cycophilin 3. Cloning and expression of eleven cyclophilin homologues from the free-living nematode Caenorhabditis elegans (C. elegans) has recently been reported. Cyclophilin 3 (Cyc-3), one of the most abundantly expressed isoforms, was chosen as the initial target for further study. The structure of the protein was solved to high resolution, allowing identification of a number of key structural features that differ from those of the archetypal cyclophilin, Cyclophilin A. These newly determined features, which may prove to be functionally significant, were used to define a new cyclophilin subfamily. Cycophilin 40. Cyclophilin 40 (Cyp 40) is a two domain immunophilin containing a conserved cyclophilin domain linked via a charged linker region to the C-terminal domain comprised largely of three copies of the tetratricopeptide repeat (TPR) motif. Cyp 40 constitutes part of the “mature” steroid hormone receptor complex, interactions with Hsp90 have been described, although the exact nature of the interaction has not been well defined. Using cloned bovine Cyp 40, two very different crystal forms were grown. FKBP22. Isolation of FKBP22 for the endoplasmic reticulum of Neurosporra crassa (N. crassa) has recently been reported. The C-terminal sequence appears to be unique among other FKBP sequences, being rather highly charged and is consistent with an amphipathic helical conformation. Crystallisation and preliminary partial X-ray structure determination of FKBP22 from N. crassa are reported.
Supervisor: Not available Sponsor: Not available
Qualification Name: Thesis (Ph.D.) Qualification Level: Doctoral
EThOS ID: uk.bl.ethos.649656  DOI: Not available
Share: