1r02
From Proteopedia
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| - | + | ==Solution structure of Human Orexin-A:Regulator of Appetite and Wakefulness== | |
| - | + | <StructureSection load='1r02' size='340' side='right' caption='[[1r02]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1r02]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R02 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1R02 FirstGlance]. <br> | |
| - | ==Disease== | + | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1cq0|1cq0]]</td></tr> |
| - | [[http://www.uniprot.org/uniprot/OREX_HUMAN OREX_HUMAN]] Defects in HCRT are the cause of narcolepsy type 1 (NRCLP1) [MIM:[http://omim.org/entry/161400 161400]]. Narcolepsy is a neurological disabling sleep disorder, characterized by excessive daytime sleepiness, sleep fragmentation, symptoms of abnormal rapid-eye-movement (REM) sleep, such as cataplexy, hypnagogic hallucinations, and sleep paralysis. Cataplexy is a sudden loss of muscle tone triggered by emotions, which is the most valuable clinical feature used to diagnose narcolepsy. Human narcolepsy is primarily a sporadically occurring disorder but familial clustering has been observed. Note=Human narcolepsy is associated with a deficient orexin system. Orexins are absent and/or greatly diminished in the brain and cerebrospinal fluid (CSF) of most narcoleptic patients.<ref>PMID:10973318</ref> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1r02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r02 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1r02 RCSB], [http://www.ebi.ac.uk/pdbsum/1r02 PDBsum]</span></td></tr> |
| - | + | </table> | |
| - | ==Function== | + | == Disease == |
| + | [[http://www.uniprot.org/uniprot/OREX_HUMAN OREX_HUMAN]] Defects in HCRT are the cause of narcolepsy type 1 (NRCLP1) [MIM:[http://omim.org/entry/161400 161400]]. Narcolepsy is a neurological disabling sleep disorder, characterized by excessive daytime sleepiness, sleep fragmentation, symptoms of abnormal rapid-eye-movement (REM) sleep, such as cataplexy, hypnagogic hallucinations, and sleep paralysis. Cataplexy is a sudden loss of muscle tone triggered by emotions, which is the most valuable clinical feature used to diagnose narcolepsy. Human narcolepsy is primarily a sporadically occurring disorder but familial clustering has been observed. Note=Human narcolepsy is associated with a deficient orexin system. Orexins are absent and/or greatly diminished in the brain and cerebrospinal fluid (CSF) of most narcoleptic patients.<ref>PMID:10973318</ref> | ||
| + | == Function == | ||
[[http://www.uniprot.org/uniprot/OREX_HUMAN OREX_HUMAN]] Neuropeptides that play a significant role in the regulation of food intake and sleep-wakefulness, possibly by coordinating the complex behavioral and physiologic responses of these complementary homeostatic functions. A broader role in the homeostatic regulation of energy metabolism, autonomic function, hormonal balance and the regulation of body fluids, is also suggested. Orexin-A binds to both OX1R and OX2R with a high affinity, whereas orexin-B binds only to OX2R with a similar high affinity. | [[http://www.uniprot.org/uniprot/OREX_HUMAN OREX_HUMAN]] Neuropeptides that play a significant role in the regulation of food intake and sleep-wakefulness, possibly by coordinating the complex behavioral and physiologic responses of these complementary homeostatic functions. A broader role in the homeostatic regulation of energy metabolism, autonomic function, hormonal balance and the regulation of body fluids, is also suggested. Orexin-A binds to both OX1R and OX2R with a high affinity, whereas orexin-B binds only to OX2R with a similar high affinity. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Orexin-A and orexin-B (hypocretin-1 and hypocretin-2, respectively) are important hypothalamic neuro-peptides, which are encoded by a single mRNA transcript and stimulate food intake as well as regulate wakefulness. Here we determined the solution structure of orexin-A by NMR spectroscopy and by simulated-annealing calculation. The structural features of orexin-A involve two alpha-helices, with the hydrophobic residues disposed to on one side of helix, and hydrophilic residues to the other. A hydrophilic turn induced by two disulfide bonds provides the key difference between orexin-A and -B. With previous mutagenic studies, the derived structure of orexin-A provides us with a structure-functional view for novel drug design. | ||
| - | + | Solution structure of human orexin-A: regulator of appetite and wakefulness.,Kim HY, Hong E, Kim JI, Lee W J Biochem Mol Biol. 2004 Sep 30;37(5):565-73. PMID:15479620<ref>PMID:15479620</ref> | |
| - | + | ||
| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | <references | + | </div> |
| - | [[Category: Hong, E | + | == References == |
| - | [[Category: Kim, H Y | + | <references/> |
| - | [[Category: Kim, J I | + | __TOC__ |
| - | [[Category: Lee, W | + | </StructureSection> |
| + | [[Category: Hong, E]] | ||
| + | [[Category: Kim, H Y]] | ||
| + | [[Category: Kim, J I]] | ||
| + | [[Category: Lee, W]] | ||
[[Category: Helix-loop-helix]] | [[Category: Helix-loop-helix]] | ||
[[Category: Neuropeptide]] | [[Category: Neuropeptide]] | ||
[[Category: Turn]] | [[Category: Turn]] | ||
Revision as of 11:51, 18 December 2014
Solution structure of Human Orexin-A:Regulator of Appetite and Wakefulness
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Categories: Hong, E | Kim, H Y | Kim, J I | Lee, W | Helix-loop-helix | Neuropeptide | Turn
