THE C-TYPE LECTIN CARBOHYDRATE RECOGNITION DOMAIN OF HUMAN TETRANECTIN
Structure of the C-type lectin carbohydrate recognition domain of human tetranectin.
Human Plasminogen Binding Protein Tetranectin: Crystallization and Preliminary X-Ray Analysis of the C-Type Lectin Crd and the Full-Length Protein
Crystal Structure of Tetranectin, a Trimeric Plasminogen-Binding Protein with an Alpha-Helical Coiled Coil
Tetranectin, a Trimeric Plasminogen-Binding C-Type Lectin
The Gene Structure of Tetranectin, a Plasminogen Binding Protein
ALQTVCLKGTKVHMKCFLAFTQTKTFHEASEDCISRGGTLSTPQTGSENDALYEYLRQSVGNEAEIWLGLNDMAAEGTWV DMTGARIAYKNWETEITAQPDGGKTENCAVLSGAANGKWFDKRCRDQLPYICQFGIV
THE PROTEIN WAS CRYSTALLIZED BY THE HANGING DROP METHOD BY MIXING 4 MICROLITER OF A SOLUTION CONTAINING 5 MG/ML PROTEIN, 0.02 M CACL2, 0.05 M NACL, 0.10 M TRIS-HCL, PH 8.0, WITH 3 MICROLITER RESERVOIR SOLUTION CONTAINING 2.1 M AMMONIUM SULFATE, 5 % ETHANOL., vapor diffusion - hanging drop
THE STRUCTURE WAS INITIALLY REFINED TO AN R-VALUE OF 34.7 % USING X-PLOR.
MOEWS AND KRETSINGER (J.MOL.BIOL. (1995) 91, 201-228)
THE CARBOHYDRATE RECOGNITION DOMAIN OF TETRANECTIN FORMS A DIMER IN CRYSTALS, WHEREAS FULL-LENGTH TETRANECTIN IS A HOMOTRIMER IN CRYSTALS AS WELL AS IN SOLUTION. TWO DIFFERENT SIDE CHAIN CONFORMATIONS HAVE BEEN IDENTIFIED FOR THR 48, VAL 49, AND MET 58. IN ADDITION, THE AMIDE MOIETIES LINKING THR 138 AND GLU 139 AND THR 141 AND ALA 142, RESPECTIVELY, ARE OBSERVED IN TWO DISTINCT CONFORMATIONS. THE SIDE CHAINS OF NINE RESIDUES (GLN 66, ARG 101, GLU 107, ARG 130, LYS 134, GLU 139, ARG 169, ILE 180, VAL 181) ARE LESS WELL-DEFINED.
TETRANECTIN, PLASMINOGEN BINDING, KRINGLE 4, C-TYPE LECTIN, CARBOHYDRATE RECOGNITION DOMAIN, LECTIN
MELWGAYLLLCLFSLLTQVTTEPPTQKPKKIVNAKKDVVNTKMFEELKSRLDTLAQEVALLKEQQALQTVCLKGTKVHMK CFLAFTQTKTFHEASEDCISRGGTLSTPQTGSENDALYEYLRQSVGNEAEIWLGLNDMAAEGTWVDMTGARIAYKNWETE ITAQPDGGKTENCAVLSGAANGKWFDKRCRDQLPYICQFGIV