1HY9

Solution structure of the satiety factor, CART, reveals new functionality of a well-known fold.

(2001) Biochemistry 40: 9082-9088

• PubMed: 11478874 Search on PubMed
• DOI: https://doi.org/10.1021/bi010433u
• Primary Citation of Related Structures:  
  1HY9


• PubMed Abstract: 
  

  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.

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Organizational Affiliation: 

Novo Nordisk A/S, Novo Allé 1, DK-2880 Bagsvaerd, Denmark. svl@novonordisk.com