Freedman, R.B. and Gane, P.J. and Hawkins, H.C. and Hlodan, R. and McLaughlin, S.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 available from this repository. (Contact us about this Publication)|
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:||29 Jun 2009 10:46|
|Resource URI:||http://kar.kent.ac.uk/id/eprint/17746 (The current URI for this page, for reference purposes)|
- Depositors only (login required):