1
Here we report the first X-ray crystal structure of a teleost IRBP, and the only structure with a bound ligand.
2
The presence of the electron density of the bound ligand may provide important clues on the likely function of NIF3-like proteins.
3
A well-defined electron density corresponding to an endogenously bound ligand of unknown identity is observed in close proximity to the metal site.
4
Our study, which provides the first structure of an IRBP with bound ligand, supports a potential role for fatty acids in regulating retinoid binding.
5
Nitrocellulose sequesters proteins and bound ligand at the site of application, whereas free ligand is mobilized by bulk movement of the solvent through capillary action.
6
Gas-phase activation inside the mass spectrometer removes the detergent to yield the isolated proteins with bound ligands.
7
A semi-automated computational procedure to assist in the identification of bound ligands from unknown electron density has been developed.
8
An analysis of the degree of folding of the bound ligands confirmed the general tendency of small molecules to bind in an extended conformation.