3E6J
Crystal Structure of Variable Lymphocyte Receptor (VLR) RBC36 in Complex with H-trisaccharide
Summary for 3E6J
| Entry DOI | 10.2210/pdb3e6j/pdb |
| Related PRD ID | PRD_900036 |
| Descriptor | Variable lymphocyte receptor diversity region, alpha-L-fucopyranose-(1-2)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, SULFATE ION, ... (5 entities in total) |
| Functional Keywords | variable lymphocyte receptors, vlr, leucine-rich repeat, lrr, adaptive immunity, immune system, sea lamprey, jawless fish, receptor |
| Biological source | Petromyzon marinus (marine lamprey) |
| Total number of polymer chains | 1 |
| Total formula weight | 26321.67 |
| Authors | Han, B.W.,Herrin, B.R.,Cooper, M.D.,Wilson, I.A. (deposition date: 2008-08-15, release date: 2008-10-07, Last modification date: 2023-08-30) |
| Primary citation | Han, B.W.,Herrin, B.R.,Cooper, M.D.,Wilson, I.A. Antigen recognition by variable lymphocyte receptors. Science, 321:1834-1837, 2008 Cited by PubMed Abstract: Variable lymphocyte receptors (VLRs) rather than antibodies play the primary role in recognition of antigens in the adaptive immune system of jawless vertebrates. Combinatorial assembly of leucine-rich repeat (LRR) gene segments achieves the required repertoire for antigen recognition. We have determined a crystal structure for a VLR-antigen complex, VLR RBC36 in complex with the H-antigen trisaccharide from human blood type O erythrocytes, at 1.67 angstrom resolution. RBC36 binds the H-trisaccharide on the concave surface of the LRR modules of the solenoid structure where three key hydrophilic residues, multiple van der Waals interactions, and the highly variable insert of the carboxyl-terminal LRR module determine antigen recognition and specificity. The concave surface assembled from the most highly variable regions of the LRRs, along with diversity in the sequence and length of the highly variable insert, can account for the recognition of diverse antigens by VLRs. PubMed: 18818359DOI: 10.1126/science.1162484 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.67 Å) |
Structure validation
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