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Millhauser Lab Department of
Chemistry & Biochemistry |
Prions, Agouti-Related
Protein |
| AgRP and Agouti... |
Prion Protein... |
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Lab Members
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| NMR
structure of the Agouti-Related Protein showing a cluster of
aromatic residues implicated in stability. AgRP is an antagonist
of melanocortin receptors in the hypothalamus that regulate energy
balance in mammals. (1hyk) |
PrP's
normal
function is likely related to copper regulation in the central nervous
system. In
full-length PrP, Cu2+ ions bind primarily in the octarepeat
domain composed of adjacent PHGGGWGQ segments.
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NMR
structure of Agouti, involved in pigmentation, identifies two
conformations controlled by cis/trans Ala-Pro isomerization (1y7j, 1y7k).
Both AgRP and Agouti adopt unusual inhibitor cystine knot fold motifs. |
Crystal
structure of the HGGGW octarepeat
copper binding site in the prion protein. (Click here for coordinates.)
This is the dominant binding mode at high Cu2+
occupancy.
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Professor
Glenn L. Millhauser
Department of Chemistry & Biochemistry
University of California, Santa Cruz
Santa Cruz, CA 95064
glennm-AT-chemistry.ucsc.edu
office phone 831 459 2176
lab phone 831 459 3390
fax 831 459 2935
Research Supported by the NIH and NSF
