Structure determination of a Galectin-3-carbohydrate complex using paramagnetism-based NMR constraints.

ABSTRACT: The determination of the location and conformation of a natural ligand bound to a protein receptor is often a first step in the rational design of molecules that can modulate receptor function. NMR observables, including NOEs, often provide the basis for these determinations. However, when ligands are carbohydrates, interactions mediated by extensive hydrogen-bonding networks often reduce or eliminate NOEs between ligand and protein protons. In these cases, it is useful to look to other distance- and orientation-dependent observables that can constrain the geometry of ligand-protein complexes. Here we illustrate the use of paramagnetism-based NMR constraints, including pseudo-contact shifts (PCS) and field-induced residual dipolar couplings (RDCs). When a paramagnetic center can be attache

SUBMITTER: Zhuang T 

PROVIDER: S-EPMC2442008 | biostudies-literature | 2008 Jul

REPOSITORIES: biostudies-literature