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.
The aim of this project was to examine the functional role of the short loop that connects the two domains of the protein neurophysin. We were specifically interested in the extent to which loop residues participated in the increase in dimerization constant associated with ligand-binding. For this we examined the effects of mutation of individual loop residues on both dimerization and peptide-binding , but needed to obtain the structure of the protein bovine neurophysin-I in both liganded and non-liganded states in order to interpret the results we obtained. Crystals of the protein in these states were obtained. Crystals of the des 1-6 derivative of the F91STOP mutant of bovine neurophysin-I in the unliganded state were submitted to NE-CAT for collection of X-ray diffraction data.
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