Intermolecular Interactions Between DMα and DMβ Proteins in BuLA‐DM Complex of Water Buffalo Bubalus bubalis
| Autor: | Deepak Panwar, Sher Ali, Leena Rawal |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Buffaloes Protein Conformation Peptide Major histocompatibility complex Biochemistry Protein–protein interaction 03 medical and health sciences 0302 clinical medicine Antigen Animals Macromolecular docking Amino Acid Sequence Molecular Biology chemistry.chemical_classification Antigen Presentation biology Histocompatibility Antigens Class II Cell Biology biology.organism_classification Blot 030104 developmental biology Gene Expression Regulation chemistry Organ Specificity Cytoplasm biology.protein Bubalus Sequence Alignment 030215 immunology |
| Zdroj: | Journal of Cellular Biochemistry. 118:4254-4266 |
| ISSN: | 1097-4644 0730-2312 |
| Popis: | The major histocompatibility complex (MHC) with its three classes represents a cluster of tightly linked genes with defined immunological and non-immunological functions. The DM, a MHC class II molecule is formed by the non-covalent association of DMα and DMβ chains. It binds with the processed peptide antigens and presents them to T lymphocytes, thereby triggering the immune responses. Startlingly, the expression pattern and structural organization of DMα and DMβ proteins in buffalo remains undefined. We isolated and purified the DMα and DMβ proteins from Bubalus bubalis using gel filtration chromatography. Employing western blotting and immunohistochemistry, highest expression of these proteins was observed in spleen and were later localized in the cytoplasm. We modelled 3D structures of the proteins and assessed the binding interface of BuLA-DM docked complex. In the process, we uncovered 9 DMα and 8 DMβ specific residues participating in the formation of BuLA-DM complex. Our work demonstrated active participation of the critical amino acid residues engaged in the formation of BuLA-DM complex facilitating deeper understanding on the structure-function relationship of these proteins. J. Cell. Biochem. 118: 4254-4266, 2017. © 2017 Wiley Periodicals, Inc. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text