3RBG
Crystal structure analysis of Class-I MHC restricted T-cell associated molecule
Summary for 3RBG
Entry DOI | 10.2210/pdb3rbg/pdb |
Descriptor | Cytotoxic and regulatory T-cell molecule, PHOSPHATE ION (3 entities in total) |
Functional Keywords | igv, crtam, structural genomics, psi-biology, new york structural genomics research consortium, nysgrc, atoms-to-animals: the immune function network, ifn, immune system |
Biological source | Homo sapiens (human) |
Cellular location | Membrane ; Single-pass type I membrane protein : O95727 |
Total number of polymer chains | 4 |
Total formula weight | 57364.71 |
Authors | Rubinstein, R.,Ramagopal, U.A.,Toro, R.,Nathenson, S.G.,Fiser, A.,Almo, S.C.,New York Structural Genomics Research Consortium (NYSGRC),Atoms-to-Animals: The Immune Function Network (IFN) (deposition date: 2011-03-29, release date: 2011-05-25, Last modification date: 2024-11-27) |
Primary citation | Rubinstein, R.,Ramagopal, U.A.,Nathenson, S.G.,Almo, S.C.,Fiser, A. Functional classification of immune regulatory proteins. Structure, 21:766-776, 2013 Cited by PubMed Abstract: The members of the immunoglobulin superfamily (IgSF) control innate and adaptive immunity and are prime targets for the treatment of autoimmune diseases, infectious diseases, and malignancies. We describe a computational method, termed the Brotherhood algorithm, which utilizes intermediate sequence information to classify proteins into functionally related families. This approach identifies functional relationships within the IgSF and predicts additional receptor-ligand interactions. As a specific example, we examine the nectin/nectin-like family of cell adhesion and signaling proteins and propose receptor-ligand interactions within this family. Guided by the Brotherhood approach, we present the high-resolution structural characterization of a homophilic interaction involving the class-I MHC-restricted T-cell-associated molecule, which we now classify as a nectin-like family member. The Brotherhood algorithm is likely to have a significant impact on structural immunology by identifying those proteins and complexes for which structural characterization will be particularly informative. PubMed: 23583034DOI: 10.1016/j.str.2013.02.022 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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