Protein Science Sheba protein
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
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 PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by HOLTET, T. L.
Right arrow Articles by ETZERODT, M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by HOLTET, T. L.
Right arrow Articles by ETZERODT, M.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Protein Science, Vol 6, Issue 7 1511-1515, Copyright © 1997 by Cold Spring Harbor Laboratory Press

ARTICLE

Tetranectin, a trimeric plasminogen-binding C-type lectin

T. L. HOLTET, J. H. GRAVERSEN, I. CLEMMENSEN, H. C. THOGERSEN and M. ETZERODT
Laboratory of Gene Expression, Department of Molecular and Structural Biology, University of Aarhus, Denmark

Tetranectin, a plasminogen-binding protein belonging to the family of C-type lectins, was expressed in E. coli and converted to its native form by in vitro refolding and proteolytic processing. Recombinant tetranectin--as well as natural tetranectin from human plasma--was shown by chemical cross-linking analysis and SDS-PAGE to be a homo-trimer in solution as are other known members of the collectin family of C-type lectins. Biochemical evidence is presented showing that an N-terminal domain encoded within exons 1 and 2 of the tetranectin gene is necessary and sufficient to govern subunit trimerization.
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
M. Hansen, T. Wind, G. E. Blouse, A. Christensen, H. H. Petersen, S. Kjelgaard, L. Mathiasen, T. L. Holtet, and P. A. Andreasen
A Urokinase-type Plasminogen Activator-inhibiting Cyclic Peptide with an Unusual P2 Residue and an Extended Protease Binding Surface Demonstrates New Modalities for Enzyme Inhibition
J. Biol. Chem., November 18, 2005; 280(46): 38424 - 38437.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. H. Graversen, R. H. Lorentsen, C. Jacobsen, S. K. Moestrup, B. W. Sigurskjold, H. C. Thogersen, and M. Etzerodt
The Plasminogen Binding Site of the C-Type Lectin Tetranectin Is Located in the Carbohydrate Recognition Domain, and Binding Is Sensitive to Both Calcium and Lysine
J. Biol. Chem., October 30, 1998; 273(44): 29241 - 29246.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. H. Graversen, C. Jacobsen, B. W. Sigurskjold, R. H. Lorentsen, S. K. Moestrup, H. C. Thogersen, and M. Etzerodt
Mutational Analysis of Affinity and Selectivity of Kringle-Tetranectin Interaction. GRAFTING NOVEL KRINGLE AFFINITY ONTO THE TETRANECTIN LECTIN SCAFFOLD
J. Biol. Chem., November 22, 2000; 275(48): 37390 - 37396.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1997 by The Protein Society.