Diversity in Hapten Recognition: Structural Study of an Anti-cocaine Antibody M82G2
Antibodies against cocaine and other drugs of abuse are the basis for diagnostic tests for the presence of those drugs in human serum. The 1.7 Å resolution crystal structure of the anti-cocaine monoclonal antibody M82G2 in complex with cocaine is presented. This structure determination was undertake...
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Published in | Journal of crystal growth Vol. 349; no. 3; pp. 570 - 582 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
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England
Elsevier Ltd
10.06.2005
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Abstract | Antibodies against cocaine and other drugs of abuse are the basis for diagnostic tests for the presence of those drugs in human serum. The 1.7
Å resolution crystal structure of the anti-cocaine monoclonal antibody M82G2 in complex with cocaine is presented. This structure determination was undertaken to establish the stereochemical features in the antibody binding site that confer specificity for cocaine, and as part of an ongoing project to understand the rules that govern molecular recognition. The cocaine-binding site can be characterized topologically as a narrow groove on the protein surface. The antibody utilizes water-mediated hydrogen bonding, and cation–π and stacking (π–π) interactions to provide specificity. Comparison with the previously published structure of the anti-cocaine antibody GNC92H2 shows that binding of a small ligand can be achieved in diverse ways, both in terms of a binding site structure/topology and protein–ligand interactions. |
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AbstractList | Antibodies against cocaine and other drugs of abuse are the basis for diagnostic tests for the presence of those drugs in human serum. The 1.7
Å resolution crystal structure of the anti-cocaine monoclonal antibody M82G2 in complex with cocaine is presented. This structure determination was undertaken to establish the stereochemical features in the antibody binding site that confer specificity for cocaine, and as part of an ongoing project to understand the rules that govern molecular recognition. The cocaine-binding site can be characterized topologically as a narrow groove on the protein surface. The antibody utilizes water-mediated hydrogen bonding, and cation–π and stacking (π–π) interactions to provide specificity. Comparison with the previously published structure of the anti-cocaine antibody GNC92H2 shows that binding of a small ligand can be achieved in diverse ways, both in terms of a binding site structure/topology and protein–ligand interactions. Antibodies against cocaine and other drugs of abuse are the basis for diagnostic tests for the presence of those drugs in human serum. The 1.7A resolution crystal structure of the anti-cocaine monoclonal antibody M82G2 in complex with cocaine is presented. This structure determination was undertaken to establish the stereochemical features in the antibody binding site that confer specificity for cocaine, and as part of an ongoing project to understand the rules that govern molecular recognition. The cocaine-binding site can be characterized topologically as a narrow groove on the protein surface. The antibody utilizes water-mediated hydrogen bonding, and cation-pi and stacking (pi-pi) interactions to provide specificity. Comparison with the previously published structure of the anti-cocaine antibody GNC92H2 shows that binding of a small ligand can be achieved in diverse ways, both in terms of a binding site structure/topology and protein-ligand interactions. |
Author | Shanafelt, Armen B. Moulin, Aaron Pozharski, Edwin Hewagama, Anura Petsko, Gregory A. Ringe, Dagmar |
Author_xml | – sequence: 1 givenname: Edwin surname: Pozharski fullname: Pozharski, Edwin organization: Rosenstiel Basic Medical Sciences Research Center, Brandeis University, 415 South Street, Waltham, MA 02454, USA – sequence: 2 givenname: Aaron surname: Moulin fullname: Moulin, Aaron organization: Rosenstiel Basic Medical Sciences Research Center, Brandeis University, 415 South Street, Waltham, MA 02454, USA – sequence: 3 givenname: Anura surname: Hewagama fullname: Hewagama, Anura organization: Roche Diagnostics Corporation, 9115 Hague Road, Indianapolis, IN 46250, USA – sequence: 4 givenname: Armen B. surname: Shanafelt fullname: Shanafelt, Armen B. organization: Roche Diagnostics Corporation, 9115 Hague Road, Indianapolis, IN 46250, USA – sequence: 5 givenname: Gregory A. surname: Petsko fullname: Petsko, Gregory A. organization: Rosenstiel Basic Medical Sciences Research Center, Brandeis University, 415 South Street, Waltham, MA 02454, USA – sequence: 6 givenname: Dagmar surname: Ringe fullname: Ringe, Dagmar email: ringe@brandeis.edu organization: Rosenstiel Basic Medical Sciences Research Center, Brandeis University, 415 South Street, Waltham, MA 02454, USA |
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Snippet | Antibodies against cocaine and other drugs of abuse are the basis for diagnostic tests for the presence of those drugs in human serum. The 1.7
Å resolution... Antibodies against cocaine and other drugs of abuse are the basis for diagnostic tests for the presence of those drugs in human serum. The 1.7A resolution... |
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SubjectTerms | 60 APPLIED LIFE SCIENCES Amino Acid Sequence Animals ANTIBODIES antibody engineering antibody structure COCAINE Cocaine - analysis Cocaine - blood Cocaine - immunology CRYSTAL GROWTH Hydrogen Bonding Immunoglobulin Fab Fragments - chemistry Immunoglobulin Fab Fragments - genetics Immunoglobulin Fab Fragments - immunology immunotherapy Ligands Mice Molecular Sequence Data national synchrotron light source Protein Binding - immunology Protein Structure, Tertiary protein–ligand interaction Static Electricity Structural Homology, Protein |
Title | Diversity in Hapten Recognition: Structural Study of an Anti-cocaine Antibody M82G2 |
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