JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
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 Huang, W.
Right arrow Articles by Gettins, P. G. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Huang, W.
Right arrow Articles by Gettins, P. G. W.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

J Biol Chem, Vol. 275, Issue 2, 1089-1094, January 14, 2000

NMR Solution Structure of the Receptor Binding Domain of Human alpha 2-Macroglobulin*

Wen Huang, Klavs DolmerDagger , Xiubei Liao§, and Peter G. W. Gettins

From the Department of Biochemistry and Molecular Biology, College of Medicine, University of Illinois at Chicago, Chicago, Illinois 60612-4316

Human alpha 2-macroglobulin-proteinase complexes bind to their receptor, the low density lipoprotein receptor-related protein (LRP), through a discrete 138-residue C-terminal receptor binding domain (RBD), which also binds to the beta -amyloid peptide. We have used NMR spectroscopy on recombinantly expressed uniformly 13C/15N-labeled human RBD to determine its three-dimensional structure in solution. Human RBD is a sandwich of two antiparallel beta -sheets, one four-strand and one five-strand, and also contains one alpha -helix of 2.5 turns and an additional 1-turn helical region. The principal alpha -helix contains two lysine residues on the outer face that are known to be essential for receptor binding. A calcium binding site (Kd ~ 11 mM) is present in the loop region at one end of the beta -sandwich. Calcium binding principally affects this loop region and does not significantly perturb the stable core structure of the domain. The structure and NMR assignments will enable us to examine in solution specific binding of RBD to domains of the receptor and to beta -amyloid peptide.

* This work was supported by Grant GM54414 from the National Institutes of Health (to P. G. W. G.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The atomic coordinates and structure factors (code 1BV8) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

Dagger Supported by a postdoctoral fellowship from the Danish Natural Science Research Council.

§ Recipient of a Junior Faculty Award from the American Cancer Society.

To whom correspondence should be addressed. Tel.: 312 996 5534; Fax: 312 413 0364; E-mail: pgettins@tigger.uic.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
Add to CiteULike CiteULike   Add to Complore Complore   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
K. Dolmer and P. G. W. Gettins
Three Complement-like Repeats Compose the Complete {alpha}2-Macroglobulin Binding Site in the Second Ligand Binding Cluster of the Low Density Lipoprotein Receptor-related Protein
J. Biol. Chem., November 10, 2006; 281(45): 34189 - 34196.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
S. Arandjelovic, C. L. Van Sant, and S. L. Gonias
Limited Mutations in Full-length Tetrameric Human {alpha}2-Macroglobulin Abrogate Binding of Platelet-derived Growth Factor-BB and Transforming Growth Factor-beta1
J. Biol. Chem., June 23, 2006; 281(25): 17061 - 17068.
[Abstract] [Full Text] [PDF]

Home page
 J. Virol.Home page
T. Rai, M. Caffrey, and L. Rong
Identification of Two Residues within the LDL-A Module of Tva That Dictate the Altered Receptor Specificity of Mutant Subgroup A Avian Sarcoma and Leukosis Viruses
J. Virol., December 1, 2005; 79(23): 14962 - 14966.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
J. M. Mettenburg, D. J. Webb, and S. L. Gonias
Distinct Binding Sites in the Structure of alpha 2-Macroglobulin Mediate the Interaction with beta -Amyloid Peptide and Growth Factors
J. Biol. Chem., April 5, 2002; 277(15): 13338 - 13345.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
K. Dolmer, W. Huang, and P. G. W. Gettins
NMR Solution Structure of Complement-like Repeat CR3 from the Low Density Lipoprotein Receptor-related Protein. EVIDENCE FOR SPECIFIC BINDING TO THE RECEPTOR BINDING DOMAIN OF HUMAN alpha 2-MACROGLOBULIN
J. Biol. Chem., February 4, 2000; 275(5): 3264 - 3269.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
L. Melman, Z.-f. Cao, S. Rennke, M. P. Marzolo, M. R. Wardell, and G. Bu
High Affinity Binding of Receptor-associated Protein to Heparin and Low Density Lipoprotein Receptor-related Protein Requires Similar Basic Amino Acid Sequence Motifs
J. Biol. Chem., July 27, 2001; 276(31): 29338 - 29346.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2000 by the American Society for Biochemistry and Molecular Biology.