The Millhauser Lab Prions, AgRP signaling, EPR, NMR
|AgRP and Agouti
|| Prion Protein
|AgRP and Agouti bind to melanocortin
receptors and control a wide range of physiological
functions, including pigmentation and metabolism.
The NMR structure of the agouti signaling protein (red),
is shown docked to the melanocortin 1 receptor.
AgRP binding to the melanocortin-4 receptor promotes the
opening of an inward rectifying potassium channel,
independent of G-proteins (Nature
Misfolding of PrPC (above) causes the prion diseases, which include kuru, CJD and mad cow disease. PrP's normal function is related to copper and zinc regulation in the central nervous system. DEER EPR shows that a high affinity Cu2+ ion, coordinated by the octarepeat domain (not shown), localizes to a surface site on the C-terminal domain (Structure 24:1057-67 2016).
Department of Chemistry & Biochemistry
University of California, Santa Cruz
Santa Cruz, CA 95064
glennm at ucsc.edu
office phone 831 459 2176
lab phone 831 459 3390
fax 831 459 2935
Research Supported by the NIH
Web design by Chloe S. Millhauser