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3E6J

Crystal Structure of Variable Lymphocyte Receptor (VLR) RBC36 in Complex with H-trisaccharide

Summary for 3E6J
Entry DOI10.2210/pdb3e6j/pdb
Related PRD IDPRD_900036
DescriptorVariable 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 Keywordsvariable lymphocyte receptors, vlr, leucine-rich repeat, lrr, adaptive immunity, immune system, sea lamprey, jawless fish, receptor
Biological sourcePetromyzon marinus (marine lamprey)
Total number of polymer chains1
Total formula weight26321.67
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: 2024-11-20)
Primary citationHan, 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: 18818359
DOI: 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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