BBSRC Portfolio Analyser
Award details
Characterisation and interactions of an Eimeria tenella protein homologous to coagulation factor XI heavy chain
Reference
BBS/E/I/00000423
Principal Investigator / Supervisor
Professor Fiona Tomley
Co-Investigators /
Co-Supervisors
Institution
The Pirbright Institute
Department
The Pirbright Institute Department
Funding type
Research
Value (£)
114,112
Status
Completed
Type
Institute Project
Start date
01/04/1997
End date
30/09/1999
Duration
30 months
Abstract
Etmic-5, a protein from the microneme organelles of E. tenella, contains eleven repeated motifs which are structurally similar to the Apple (A) domains of blood coagulation factor XI and plasma prekallikrein. Apple domains are responsible for adhesive interactions mediated by these proteins via specific ligand-binding interactions. Parasite exoxytic organelles contain many proteins and it has been postulated that the active structure which interacts with the host cell may be an aggregate arranged to integrate into a pre- existing plasma membrane. Since Mic5 has a structure which suggests it may bind multiple ligands, this protein may prove to be critical in the invasion process. The aims of this project are to investigate structural and functional aspects of individual domains of the E. tenella protein.
Summary
unavailable
Committee
Closed Committee - Biochemistry & Cell Biology (BCB)
Research Topics
X – not assigned to a current Research Topic
Research Priority
X – Research Priority information not available
Research Initiative
X - not in an Initiative
Funding Scheme
X – not Funded via a specific Funding Scheme
I accept the
terms and conditions of use
(opens in new window)
export PDF file
back to list
new search