SOLUTION STRUCTURE OF THE SYNDECAN-4 WHOLE CYTOPLASMIC DOMAIN
Solution structure of the dimeric cytoplasmic domain of syndecan-4.
Solution Structure of a Syndecan-4 Cytoplasmic Domain and Its Interaction with Phosphatidylinositol 4,5-Bisphosphate
AMPHIGLYCAN, RYUDOCAN CORE PROTEIN, SYND4
Solution structure of the Syndecan-4 whole cytoplasmic domain in the presence of phosphatidylinositol 4,5-bisphosphate
This peptide was chemically synthesized. The sequence of this petide occurs naturally in humans (Homo Sapiens).
This structure was determined using standard 2D homonuclear techniques.
The structures are based on a total of 306 restraints, 246 are intramonomer NOE-derived distance constraints, 48 intermonomer NOE-derived distance restraints and 12 dihedral angle restraints.
2-4mM Syndecan-4 peptide ; 50mM phosphate buffer; 90% H2O, 10% D2O
2-4mM Syndecan-4 peptide ; 50mM phosphate buffer; 100% D2O
symmetric-parallel-interwinded dimer, SIGNALING PROTEIN