This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Galectin-3 is a galactose-binding mammalian protein with suggested involvement in a variety of processes, including cell-cell and cell-matrix interactions, which modulate metastasis of malignant cells. The carbohydrate recognition domain is structurally related to galectin-1, but it exhibits distinct association properties that are dependent on a proline-rich N-terminal domain. There is substantial interest in structurally characterizing ligand interactions and bound-ligand geometries as a basis for the design of possible anti-cancer drugs. Standard NMR methodologies, such as those giving inter-proton distance constraints from transferred NOE data, yield some useful results, but numbers of constraints can be small when carbohydrate ligands are involved. This collaborative project will provide additional orientational constraints using new NMR methodology that measures residual dipolar couplings (RDCs) from bound ligands in field oriented media.
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