Freedman, Robert B. and Gane, Paul J. and Hawkins, Hilary C. and Hlodan, R. and McLaughlin, Stephen H. and Parry, J.W.L. (1998) Experimental and theoretical analyses of the domain architecture of mammalian protein disulphide-isomerase. Biological Chemistry, 379 (3). pp. 321-328. ISSN 1431-6730. (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)
The high resolution structure of full-length protein disulphide-isomerase (PDI) has not been determined, but the polypeptide is generally assumed to comprise a series of consecutive domains. Models of its domain organisation have been proposed on the basis of various sequence-based criteria and, more recently, from structural studies on recombinant fragments corresponding to putative domains. We here describe direct studies of the domain architecture of full-length mammalian PDI based on limited proteolysis of the native enzyme. The results are consistent with an emerging model based on the existence of 4 consecutive domains each with the thioredoxin fold. The model was further tested by expressing recombinant fragments corresponding to alternative domain models and to truncated domains; the observed properties of these purified fragments supported the 4-domain model. A multiple alignment of many PDI-like sequences was generated to test whether domain boundaries could be predicted from any features of the alignment, such as sequence variability or hydrophilicity; neither of these parameters reliably predicted the domain boundaries determined by experiment.
|Subjects:||Q Science > QH Natural history > QH301 Biology|
|Divisions:||Faculties > Science Technology and Medical Studies > School of Biosciences|
|Depositing User:||R.F. Xu|
|Date Deposited:||29 Jun 2009 10:46|
|Last Modified:||09 Jul 2014 09:17|
|Resource URI:||https://kar.kent.ac.uk/id/eprint/17746 (The current URI for this page, for reference purposes)|