1hy9
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1hy9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hy9 OCA], [http://www.ebi.ac.uk/pdbsum/1hy9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1hy9 RCSB]</span> | ||
}} | }} | ||
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[[Category: cysteine knot]] | [[Category: cysteine knot]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:11:58 2008'' |
Revision as of 18:11, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
COCAINE AND AMPHETAMINE REGULATED TRANSCRIPT
Overview
Cocaine and amphetamine regulated transcript (CART) peptide has been shown to be an anorectic peptide that inhibits both normal and starvation-induced feeding and completely blocks the feeding response induced by neuropeptide Y and regulated by leptin in the hypothalamus. The C-terminal part containing the three disulfide bridges CART(48-89) is the biologically active part of the molecule affecting food intake. The solution structure of the active part of CART has a fold equivalent to other functionally distinct small proteins. CART consists mainly of turns and loops spanned by a compact framework composed by a few small stretches of antiparallel beta-sheet common to cystine knots.
About this Structure
1HY9 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of the satiety factor, CART, reveals new functionality of a well-known fold., Ludvigsen S, Thim L, Blom AM, Wulff BS, Biochemistry. 2001 Aug 7;40(31):9082-8. PMID:11478874
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