Antibody-ligand docking: Insights into peptide-carbohydrate mimicry
Despite the enormous clinical importance for xenotransplantation, very little is known about the 3D structural basis for natural antibody recognition of the major carbohydrate xenoantigen, its derivatives and their peptide counterparts. Fundamentally, understanding the nature of peptide-carbohydrate...
| Main Authors: | , , |
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| Format: | Journal Article |
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Taylor & Francis
2008
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| Online Access: | http://hdl.handle.net/20.500.11937/45145 |
| _version_ | 1848757201735254016 |
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| author | Yuriev, E. Sandrin, M. Ramsland, Paul |
| author_facet | Yuriev, E. Sandrin, M. Ramsland, Paul |
| author_sort | Yuriev, E. |
| building | Curtin Institutional Repository |
| collection | Online Access |
| description | Despite the enormous clinical importance for xenotransplantation, very little is known about the 3D structural basis for natural antibody recognition of the major carbohydrate xenoantigen, its derivatives and their peptide counterparts. Fundamentally, understanding the nature of peptide-carbohydrate cross-reactivity is necessary to allow a rational design of useful inhibitors. To satisfy this need, we have initiated a project to investigate the structural aspects of antibody recognition of carbohydrate xenoantigens and their peptide mimics by molecular docking. We aim to analyse critical ligand-protein interactions with a focus on identifying the degree of structural carbohydrate mimicry exhibited by peptide ligands. In this paper, we present docking simulations of complexes between a prototypical xenoreactive monoclonal antibody and two ligands: the major carbohydrate xenoantigen, terminal galactose-(1,3)-galactose epitope [Gal(1,3)Gal] and a peptide inhibitor Galpep1 (DAHWESWL). |
| first_indexed | 2025-11-14T09:24:20Z |
| format | Journal Article |
| id | curtin-20.500.11937-45145 |
| institution | Curtin University Malaysia |
| institution_category | Local University |
| last_indexed | 2025-11-14T09:24:20Z |
| publishDate | 2008 |
| publisher | Taylor & Francis |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | curtin-20.500.11937-451452017-09-13T14:17:04Z Antibody-ligand docking: Insights into peptide-carbohydrate mimicry Yuriev, E. Sandrin, M. Ramsland, Paul Despite the enormous clinical importance for xenotransplantation, very little is known about the 3D structural basis for natural antibody recognition of the major carbohydrate xenoantigen, its derivatives and their peptide counterparts. Fundamentally, understanding the nature of peptide-carbohydrate cross-reactivity is necessary to allow a rational design of useful inhibitors. To satisfy this need, we have initiated a project to investigate the structural aspects of antibody recognition of carbohydrate xenoantigens and their peptide mimics by molecular docking. We aim to analyse critical ligand-protein interactions with a focus on identifying the degree of structural carbohydrate mimicry exhibited by peptide ligands. In this paper, we present docking simulations of complexes between a prototypical xenoreactive monoclonal antibody and two ligands: the major carbohydrate xenoantigen, terminal galactose-(1,3)-galactose epitope [Gal(1,3)Gal] and a peptide inhibitor Galpep1 (DAHWESWL). 2008 Journal Article http://hdl.handle.net/20.500.11937/45145 10.1080/08927020701665995 Taylor & Francis restricted |
| spellingShingle | Yuriev, E. Sandrin, M. Ramsland, Paul Antibody-ligand docking: Insights into peptide-carbohydrate mimicry |
| title | Antibody-ligand docking: Insights into peptide-carbohydrate mimicry |
| title_full | Antibody-ligand docking: Insights into peptide-carbohydrate mimicry |
| title_fullStr | Antibody-ligand docking: Insights into peptide-carbohydrate mimicry |
| title_full_unstemmed | Antibody-ligand docking: Insights into peptide-carbohydrate mimicry |
| title_short | Antibody-ligand docking: Insights into peptide-carbohydrate mimicry |
| title_sort | antibody-ligand docking: insights into peptide-carbohydrate mimicry |
| url | http://hdl.handle.net/20.500.11937/45145 |