Protein Science
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 ORLANDINI, M.
Right arrow Articles by OLIVIERO, S.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by ORLANDINI, M.
Right arrow Articles by OLIVIERO, S.
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 3, Issue 9 1476-1484, Copyright © 1994 by Cold Spring Harbor Laboratory Press

ARTICLE

Cloning, characterization, and modeling of a monoclonal anti-human transferrin antibody that competes with the transferrin receptor

M. ORLANDINI, A. SANTUCCI, A. TRAMONTANO, P. NERI and S. OLIVIERO
Department of Molecular Biology, University of Siena, Siena, Italy Immunobiology Research Institute Siena (IRIS), Siena, Italy

In this report we describe the isolation and characterization of a monoclonal antibody against human serum transferrin (Tf) and the cloning and sequencing of its cDNA. The antibody competes with the transferrin receptor (TR) for binding to human Tf and is therefore expected to bind at or very close to a region of interaction between Tf and its receptor. From the deduced amino acid sequence, we constructed a 3-dimensional model of the variable domains of the antibody based on the canonical structure model for the hypervariable loops. The proposed structure of the antibody is a first step toward a more detailed characterization of the antibody-Tf complex and possibly toward a better understanding of the Tf interaction with its receptor. The model might prove useful in guiding site-directed mutagenesis studies, simplifying the experimental elucidation of the antibody structure, and in the use of automatic procedures to dock the interacting molecules as soon as structural information about the structure of the human Tf molecule will be available.
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
 Biophys. JHome page
S. Mohan, N. Sinha, and S. J. Smith-Gill
Modeling the Binding Sites of Anti-Hen Egg White Lysozyme Antibodies HyHEL-8 and HyHEL-26: An Insight into the Molecular Basis of Antibody Cross-Reactivity and Specificity
Biophys. J., November 1, 2003; 85(5): 3221 - 3236.
[Abstract] [Full Text] [PDF]

Home page
 CVIHome page
J. A. D. Navoa, S. Laal, L.-A. Pirofski, G. R. McLean, Z. Dai, J. B. Robbins, R. Schneerson, A. Casadevall, and A. Glatman-Freedman
Specificity and Diversity of Antibodies to Mycobacterium tuberculosis Arabinomannan
Clin. Vaccine Immunol., January 1, 2003; 10(1): 88 - 94.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1994 by The Protein Society.