The Millhauser Lab    Prions, AgRP signaling, EPR, NMR

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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 520:94-98  2015).

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).

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Professor Glenn L. Millhauser
Department of Chemistry & Biochemistry
University of California, Santa Cruz
Santa Cruz, CA 95064

glennm at

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