View source for 2m76


==Structure of the Regulatory Domain of Human Brain Carnitine Palmitoyltransferase 1==
<StructureSection load='2m76' size='340' side='right'caption='[[2m76]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2m76]] 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=2M76 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2M76 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2m76 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2m76 OCA], [https://pdbe.org/2m76 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2m76 RCSB], [https://www.ebi.ac.uk/pdbsum/2m76 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2m76 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CPT1C_HUMAN CPT1C_HUMAN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Neurons contain a mammalian-specific isoform of the enzyme carnitine palmitoyltransferase 1 (CPT1C) that couples malonyl-CoA to ceramide levels thereby contributing to systemic energy homeostasis and feeding behavior. In contrast to CPT1A, which controls the rate-limiting step of long-chain fatty acid beta-oxidation in all tissues, the biochemical context and regulatory mechanism of CPT1C are unknown. CPT1 enzymes are comprised of an N-terminal regulatory domain and a C-terminal catalytic domain that are separated by two transmembrane helices. In CPT1A, the regulatory domain, termed N, adopts an inhibitory and non-inhibitory state, Nalpha and Nbeta, respectively, which differ in their association with the catalytic domain. To provide insight into the regulatory mechanism of CPT1C, we have determined the structure of its regulatory domain (residues Met1-Phe50) by NMR spectroscopy. In relation to CPT1A, the inhibitory Nalpha state was found to be structurally homologues whereas the non-inhibitory Nbeta state was severely destabilized, suggesting a change in overall regulation. The destabilization of Nbeta may contribute to the low catalytic activity of CPT1C relative to CPT1A and makes its association with the catalytic domain unlikely. In analogy to the stabilization of Nbeta by the CPT1A catalytic domain, non-inhibitory interactions of N of CPT1C with another protein may exist. (c) 2013 Wiley Periodicals, Inc. Biopolymers, 2013.

Structural characterization of the regulatory domain of brain carnitine palmitoyltransferase 1.,Samanta S, Situ AJ, Ulmer TS Biopolymers. 2013 Aug 27. doi: 10.1002/bip.22396. PMID:24037959<ref>PMID:24037959</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2m76" style="background-color:#fffaf0;"></div>

==See Also==
*[[Carnitine palmitoyltransferase|Carnitine palmitoyltransferase]]
== References ==
<references/>
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Samanta S]]
[[Category: Situ AJ]]
[[Category: Ulmer TS]]