5UF1
Crystal Structure of Variable Lymphocyte Receptor (VLR) O13 in complex with H-trisaccharide
Summary for 5UF1
| Entry DOI | 10.2210/pdb5uf1/pdb |
| Related | 5EUI 5UF4 5UFB 5UFC 5UFD 5UFF |
| Related PRD ID | PRD_900036 |
| Descriptor | O13, alpha-L-fucopyranose-(1-2)-beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | variable lymphocyte receptors, vlr, leucine-rich repeat, lrr, adaptive immunity, immune system, sea lamprey, jawless fish, receptor, glycan binding, glycan receptor |
| Biological source | Petromyzon marinus (Sea lamprey) |
| Total number of polymer chains | 2 |
| Total formula weight | 55756.87 |
| Authors | Gunn, R.J.,Collins, B.C.,McKitrick, T.R.,Cummings, R.D.,Cooper, M.D.,Herrin, B.R.,Wilson, I.A. (deposition date: 2017-01-03, release date: 2017-10-18, Last modification date: 2023-10-04) |
| Primary citation | Collins, B.C.,Gunn, R.J.,McKitrick, T.R.,Cummings, R.D.,Cooper, M.D.,Herrin, B.R.,Wilson, I.A. Structural Insights into VLR Fine Specificity for Blood Group Carbohydrates. Structure, 25:1667-1678.e4, 2017 Cited by PubMed Abstract: High-quality reagents to study and detect glycans with high specificity for research and clinical applications are severely lacking. Here, we structurally and functionally characterize several variable lymphocyte receptor (VLR)-based antibodies from lampreys immunized with O erythrocytes that specifically recognize the blood group H-trisaccharide type II antigen. Glycan microarray analysis and biophysical data reveal that these VLRs exhibit greater specificity for H-trisaccharide compared with the plant lectin UEA-1, which is widely used in blood typing. Among these antibodies, O13 exhibits superior specificity for H-trisaccharide, the basis for which is revealed by comparative analysis of high-resolution VLR:glycan crystal structures. Using a structure-guided approach, we designed an O13 mutant with further enhanced specificity for H-trisaccharide. These insights into glycan recognition by VLRs suggest that lampreys can produce highly specific glycan antibodies, and are a valuable resource for the production of next-generation glycan reagents for biological and biomedical research and as diagnostics and therapeutics. PubMed: 28988747DOI: 10.1016/j.str.2017.09.003 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.03 Å) |
Structure validation
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