Carr, Mark D., Bloemink, Marieke J., Dentten, Ellen, Whelan, Adam, Gordon, Stephen V., Kelly, Geoff, Frenkiel, Tom A., Hewinson, R. Glyn, Williamson, Richard A. (2003) Solution structure of the Mycobacterium tuberculosis complex protein MPB70: from tuberculosis pathogenesis to inherited human corneal desease. Journal of Biological Chemistry, 278 . pp. 43736-43743. ISSN 0021-9258. E-ISSN 1083-351X. (Access to this publication is currently restricted. You may be able to access a copy if URLs are provided) (KAR id:77)
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Official URL: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=... |
Abstract
The closely related mycobacteria responsible for tuberculosis produce an unusually high number of secreted proteins, many of which are clearly implicated in pathogenesis and protective immunity. Falling within this category are the closely related proteins MPB70 and MPB83. The structure of MPB70 reveals a complex and novel bacterial fold, which has clear structural homology to the two C-terminal FAS1 domains of the cell adhesion protein fasciclin I, whose structures were reported very recently. Assessment of the surface features of MPB70, the sequence divergence between MPB70 and MPB83, the conservation of residues across a group of FAS1 domains, and the locations of disease-inducing mutations in betaig-h3 strongly suggests that MPB70 and MPB83 contain two functional surfaces on opposite faces, which are probably involved in binding to host cell proteins. This analysis also suggests that these functional surfaces are retained in the FAS1 proteins associated with mediating interactions between cells and the extracellular matrix (fasciclin I, periostin, and betaig-h3) and furthermore that some of the human corneal disease-inducing substitutions identified in betaig-h3 will perturb interactions at these sites.
Item Type: | Article |
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Subjects: | Q Science |
Divisions: | Divisions > Division of Natural Sciences > Biosciences |
Depositing User: | Susan Davies |
Date Deposited: | 19 Dec 2007 17:54 UTC |
Last Modified: | 16 Nov 2021 09:38 UTC |
Resource URI: | https://kar.kent.ac.uk/id/eprint/77 (The current URI for this page, for reference purposes) |
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