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New page: left|200px<br /> <applet load="1hy9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hy9" /> '''COCAINE AND AMPHETAMINE REGULATED TRANSCRIP...
 
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[[Image:1hy9.gif|left|200px]]<br />
<applet load="1hy9" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1hy9" />
'''COCAINE AND AMPHETAMINE REGULATED TRANSCRIPT'''<br />


==Overview==
==COCAINE AND AMPHETAMINE REGULATED TRANSCRIPT==
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.
<StructureSection load='1hy9' size='340' side='right'caption='[[1hy9]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1hy9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HY9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1HY9 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 10 models</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1hy9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1hy9 OCA], [https://pdbe.org/1hy9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1hy9 RCSB], [https://www.ebi.ac.uk/pdbsum/1hy9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1hy9 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CART_HUMAN CART_HUMAN] Satiety factor closely associated with the actions of leptin and neuropeptide y; this anorectic peptide inhibits both normal and starvation-induced feeding and completely blocks the feeding response induced by neuropeptide Y and regulated by leptin in the hypothalamus. It promotes neuronal development and survival in vitro.<ref>PMID:9590691</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hy/1hy9_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1hy9 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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==
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<ref>PMID:11478874</ref>
1HY9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HY9 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=11478874 11478874]
</div>
<div class="pdbe-citations 1hy9" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Blom, A.M.]]
[[Category: Blom AM]]
[[Category: Ludvigsen, S.]]
[[Category: Ludvigsen S]]
[[Category: Thim, L.]]
[[Category: Thim L]]
[[Category: Wulff, B.S.]]
[[Category: Wulff BS]]
[[Category: cysteine knot]]
 
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Retrieved from "https://proteopedia.org/1hy9"