Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow FREE Full Text (PDF) Freely available
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (11)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Symons, A.
Right arrow Articles by Barclay, A.N.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Symons, A.
Right arrow Articles by Barclay, A.N.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Protein Engineering, Vol. 12, No. 10, 885-892, October 1999
© 1999 Oxford University Press

Domain organization of the extracellular region of CD45

Antony Symons1, Antony C. Willis2 and A.Neil Barclay3

MRC Cellular Immunology Unit, Sir William Dunn School of Pathology, University of Oxford, Oxford, OX1 3RE and 2 Medical Research Council Immunochemistry Unit, Biochemistry Department, University of Oxford, Oxford, OX1 3QU, UK

CD45 is a large, heavily glycosylated, transmembrane protein phosphotyrosine phosphatase found on all nucleated cells of haematopoietic origin. In lymphocytes, the cytoplasmic phosphatase is necessary for efficient signalling through the antigen receptor but in contrast little is known about the interactions of the extracellular region of the molecule. This consists of a mucin-like region, a novel cysteine-containing region and a region containing three putative fibronectin type III domains. To confirm this organization and to identify parts potentially important for function, we have expressed fragments of the extracellular domain of rat CD45 as recombinant soluble proteins. Proteins corresponding to two, three and four domains of CD45 were expressed in secreted forms. Single domains and constructs for proteins with truncations of the predicted domains were not expressed. This is consistent with the proposed structural organization. Determination of the positions of the disulphide bonds in the N-terminal cysteine-containing region and the first fibronectin type III domain identified novel disulphide bonds within the fibronectin type III domain and an unusual inter-domain disulphide linkage. Circular dichroism spectroscopy indicated that this region of rat CD45 has mainly ß-strand secondary structure and no {alpha}-helical content. These studies support the proposed domain organization of CD45.

Keywords: CD45/cell surface proteins/domain/fibronectin type 3/phosphatase

1 Present address: The R.W.Johnson Pharmaceutical Research Institute, 3535 General Atomics Center, La Jolla, California, USA

3 To whom correspondence should be addressed; email: barclay{at}molbiol.ox.ac.uk


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 J. Immunol.Home page
E. Z. Tchilian, D. L. Wallace, R. S. Wells, D. R. Flower, G. Morgan, and P. C. L. Beverley
A Deletion in the Gene Encoding the CD45 Antigen in a Patient with SCID
J. Immunol., January 15, 2001; 166(2): 1308 - 1313.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.