1hy9
From Proteopedia
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| - | [[Image:1hy9.jpg|left|200px]] | + | [[Image:1hy9.jpg|left|200px]] |
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| - | '''COCAINE AND AMPHETAMINE REGULATED TRANSCRIPT''' | + | {{Structure |
| + | |PDB= 1hy9 |SIZE=350|CAPTION= <scene name='initialview01'>1hy9</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''COCAINE AND AMPHETAMINE REGULATED TRANSCRIPT''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1HY9 is a [ | + | 1HY9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HY9 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11478874 11478874] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: cysteine knot]] | [[Category: cysteine knot]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:43:03 2008'' |
Revision as of 09:43, 20 March 2008
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| 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
Page seeded by OCA on Thu Mar 20 11:43:03 2008
