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.

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
3P41RR015301-05S1
Application #
7369544
Study Section
Special Emphasis Panel (ZRG1)
Project Start
2005-06-01
Project End
2007-05-31
Budget Start
2005-06-01
Budget End
2007-05-31
Support Year
5
Fiscal Year
2006
Total Cost
$1,331
Indirect Cost
Name
Cornell University
Department
Chemistry
Type
Schools of Arts and Sciences
DUNS #
872612445
City
Ithaca
State
NY
Country
United States
Zip Code
14850
Chen, Wenyang; Mandali, Sridhar; Hancock, Stephen P et al. (2018) Multiple serine transposase dimers assemble the transposon-end synaptic complex during IS607-family transposition. Elife 7:
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