1cq0
From Proteopedia
(Difference between revisions)
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| - | + | ==SOLUTION STRUCTURE OF A HUMAN HYPOCRETIN-2/OREXIN-B'SOLUTION STRUCTURE OF A HUMAN HYPOCRETIN-2/OREXIN-B '== | |
| - | + | <StructureSection load='1cq0' size='340' side='right' caption='[[1cq0]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1cq0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CQ0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CQ0 FirstGlance]. <br> | |
| - | ==Disease== | + | </td></tr><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=1cq0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cq0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cq0 RCSB], [http://www.ebi.ac.uk/pdbsum/1cq0 PDBsum]</span></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> | + | </table> |
| - | + | == Disease == | |
| - | ==Function== | + | [[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 (also called hypocretin-1 and hypocretin-2, respectively) are novel hypothalamic neuropeptides encoded by a single mRNA transcript; they stimulate food intake. We have determined the three-dimensional solution structure of human hypocretin-2/orexin-B using two-dimensional 1H-NMR data and dynamical simulated annealing calculations. On the basis of NOEs, 3JHNalpha coupling constants and hydrogen-deuterium exchange rates together with chemical shift indices, human hypocretin-2/orexin-B was deduced to consist of two alpha-helices connected with a short linker in both H2O and 30% trifluoroethanol solutions. The helical axis of helix I is oriented about 60-80 degrees relative to helix II. Hybrid distance geometry and simulated-annealing protocols were used to generate an ensemble of 30 structures with no constraint violations greater than 0.03 nm for distances and 3 degrees for angles. In addition, human hypocretin-2/orexin-B shares a similar secondary-structural motif with human neuropeptide Y. This result can form the basis for further study on ligand-receptor recognition of human orexin receptors. | ||
| - | + | Solution structure of a new hypothalamic neuropeptide, human hypocretin-2/orexin-B.,Lee JH, Bang E, Chae KJ, Kim JY, Lee DW, Lee W Eur J Biochem. 1999 Dec;266(3):831-9. PMID:10583376<ref>PMID:10583376</ref> | |
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| - | == | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| - | <references | + | </div> |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Bang, E J | + | [[Category: Bang, E J]] |
| - | [[Category: Chae, K J | + | [[Category: Chae, K J]] |
| - | [[Category: Lee, D W | + | [[Category: Lee, D W]] |
| - | [[Category: Lee, K H | + | [[Category: Lee, K H]] |
| - | [[Category: Lee, W | + | [[Category: Lee, W]] |
[[Category: De novo protein]] | [[Category: De novo protein]] | ||
[[Category: Human hcrt-2/ox-b]] | [[Category: Human hcrt-2/ox-b]] | ||
Revision as of 11:35, 18 December 2014
SOLUTION STRUCTURE OF A HUMAN HYPOCRETIN-2/OREXIN-B'SOLUTION STRUCTURE OF A HUMAN HYPOCRETIN-2/OREXIN-B '
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