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 (1)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Tenette-Souaille, C.
Right arrow Articles by Smith, J. C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Tenette-Souaille, C.
Right arrow Articles by Smith, J. C.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Protein Engineering, Vol. 13, No. 5, 345-351, May 2000
© 2000 Oxford University Press

Structure of the M{alpha}2-3 toxin {alpha} antibody–antigen complex: combination of modelling with functional mapping experimental results

Catherine Tenette-Souaille1,2 and Jeremy C. Smith1,3,4

1 Section de Biophysique des Protéines et des Membranes, DBCM, CEN-Saclay, 91191 Gif-sur-Yvette, France and 3 Lehrstuhl für Biocomputing, IWR, Universität Heidelberg, Im Neuenheimer Feld 368, D-69120 Heidelberg, Germany

Modelled structures of the acetylcholine receptor-mimicking antibody, M{alpha}2-3, both free and bound to its antigen, toxin {alpha}, are assessed in the light of new experimental mutational data from functional mapping of the paratopic region of M{alpha}2-3. The experimental results are consistent with the previously-predicted structure of the free antibody, and also demonstrate that structural particularities of the M{alpha}2-3 combining site that were identified in the models play a role in the protein association. The modelled conformations of the hypervariable loops are discussed in the context of recent new data and analyses. The new mutational data allow several previously-considered modelled structures of the complex to be rejected. Two quite similar models now remain.


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




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.