Proceedings of the National Academy of Sciences of the United States of America
Structural basis for sulfation-dependent self-glycan recognition by the human immune-inhibitory receptor Siglec-8.

numbering corresponds to mature protein sequence
Construct includes Siglec-8 residues M1-H139 (carrying a C26S point mutation to enable soluble expression; numbering corresponds to mature protein), followed by six non-native C-terminal residues G140-R145 (remainder of the thrombin cleavage site after affinity-tag removal)

Insert encoding for Siglec-8 lectin domain including residues M1-H139 (carrying C26S point mutation).
Construct design described in:
Proepster, J.M., et al, Protein Expr. Purif. 2015, 109C: 14-22

Full-lenght cDNA clone: IRAUp969G05104D(imaGenes GmbH, Germany);

NMR structure of human I-type lectin domain

2D 1H-13C constant-time HSQC to obtain stereospecific assignments of Val/Leu methyls

Structural basis of human Siglec-8-carbohydrate recognition
simulated annealing and automated NOE assignment
Sialic acid-binding immunoglobulin-like lectin 8
protein backbone torsion angle prediction from NMR chemical shifts
Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman