دورية أكاديمية
High-resolution structure of HLA-A*0201 in complex with a tumour-specific antigenic peptide encoded by the MAGE-A4 gene.
العنوان: | High-resolution structure of HLA-A*0201 in complex with a tumour-specific antigenic peptide encoded by the MAGE-A4 gene. |
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المؤلفون: | Hillig RC; Institut für Immungenetik, Universitätsklinikum Charité, Humboldt-Universität zu Berlin, Germany., Coulie PG, Stroobant V, Saenger W, Ziegler A, Hülsmeyer M |
المصدر: | Journal of molecular biology [J Mol Biol] 2001 Jul 27; Vol. 310 (5), pp. 1167-76. |
نوع المنشور: | Journal Article; Research Support, Non-U.S. Gov't |
اللغة: | English |
بيانات الدورية: | Publisher: Elsevier Country of Publication: Netherlands NLM ID: 2985088R Publication Model: Print Cited Medium: Print ISSN: 0022-2836 (Print) Linking ISSN: 00222836 NLM ISO Abbreviation: J Mol Biol Subsets: MEDLINE |
أسماء مطبوعة: | Publication: Amsterdam : Elsevier Original Publication: 1959- : London : Academic Press |
مواضيع طبية MeSH: | Antigens, Neoplasm/*chemistry , Antigens, Neoplasm/*metabolism , HLA-A Antigens/*chemistry , HLA-A Antigens/*metabolism , Peptide Fragments/*chemistry , Peptide Fragments/*metabolism, Amino Acid Sequence ; Antigens, Neoplasm/genetics ; Antigens, Neoplasm/immunology ; Binding Sites ; Circular Dichroism ; Crystallography, X-Ray ; Epitopes, T-Lymphocyte/chemistry ; Epitopes, T-Lymphocyte/immunology ; HLA-A Antigens/immunology ; Humans ; Immunotherapy ; Ligands ; Models, Molecular ; Neoplasm Proteins/chemistry ; Neoplasm Proteins/genetics ; Neoplasm Proteins/immunology ; Neoplasm Proteins/metabolism ; Peptide Fragments/immunology ; Polyethylene Glycols/chemistry ; Polyethylene Glycols/metabolism ; Protein Binding ; Protein Conformation ; Protein Denaturation ; Receptors, Antigen, T-Cell/immunology ; Temperature ; Thermodynamics ; beta 2-Microglobulin/chemistry ; beta 2-Microglobulin/metabolism |
مستخلص: | The heterotrimeric complex of the human major histocompatibity complex (MHC) molecule HLA-A*0201, beta2-microglobulin and the decameric peptide GVYDGREHTV derived from the melanoma antigen (MAGE-A4 protein has been determined by X-ray crystallography at 1.4 A resolution. MAGE-A4 belongs to a family of genes that are specifically expressed in a variety of tumours. MAGE-A4-derived peptides are presented by MHC molecules at the cell surface to cytotoxic T-lymphocytes. As the HLA-A*0201:MAGE-A4 complex occurs only on tumour cells, it is considered to be an appropriate target for immunotherapy. The structure presented here reveals potential epitopes specific to the complex and indicates which peptide residues could be recognised by T-cell receptors. In addition, as the structure could be refined anisotropically, it was possible to describe the movements of the bound peptide in more detail. |
سلسلة جزيئية: | PDB 1I4F |
المشرفين على المادة: | 0 (Antigens, Neoplasm) 0 (Epitopes, T-Lymphocyte) 0 (HLA-A Antigens) 0 (Ligands) 0 (MAGEA4 protein, human) 0 (Neoplasm Proteins) 0 (Peptide Fragments) 0 (Receptors, Antigen, T-Cell) 0 (beta 2-Microglobulin) 3WJQ0SDW1A (Polyethylene Glycols) |
تواريخ الأحداث: | Date Created: 20010815 Date Completed: 20010823 Latest Revision: 20181130 |
رمز التحديث: | 20240628 |
DOI: | 10.1006/jmbi.2001.4816 |
PMID: | 11502003 |
قاعدة البيانات: | MEDLINE |
تدمد: | 0022-2836 |
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DOI: | 10.1006/jmbi.2001.4816 |