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5UFB

Crystal Structure of Variable Lymphocyte Receptor (VLR) Tn4-22 (Apo)

Summary for 5UFB
Entry DOI10.2210/pdb5ufb/pdb
Related5UEI 5UF1 5UF4 5UFC 5UFD 5UFF
DescriptorTn4-22 (2 entities in total)
Functional Keywordsvariable lymphocyte receptors, vlr, leucine-rich repeat, lrr, adaptive immunity, immune system, sea lamprey, jawless fish, receptor, glycan binding, glycan receptor
Biological sourcePetromyzon marinus (Sea lamprey)
Total number of polymer chains1
Total formula weight27718.57
Authors
Collins, B.C.,Gunn, R.J.,McKitrick, T.R.,Cummings, R.D.,Cooper, M.D.,Herrin, B.R.,Wilson, I.A. (deposition date: 2017-01-04, release date: 2017-10-18, Last modification date: 2024-11-06)
Primary citationCollins, 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: 28988747
DOI: 10.1016/j.str.2017.09.003
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.844 Å)
Structure validation

227344

數據於2024-11-13公開中

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