1r02: Difference between revisions

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-[[Image:1r02.gif|left|200px]]
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-{{STRUCTURE_1r02|  PDB=1r02  |  SCENE=  }}
-'''Solution structure of Human Orexin-A:Regulator of Appetite and Wakefulness'''
+==Solution structure of Human Orexin-A:Regulator of Appetite and Wakefulness==
+<StructureSection load='1r02' size='340' side='right'caption='[[1r02]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1r02]] 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=1R02 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1R02 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 1 model</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=1r02 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r02 OCA], [https://pdbe.org/1r02 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1r02 RCSB], [https://www.ebi.ac.uk/pdbsum/1r02 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1r02 ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/OREX_HUMAN OREX_HUMAN] Defects in HCRT are the cause of narcolepsy type 1 (NRCLP1) [MIM:[https://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 ==
+[https://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.
-==Overview==
+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>
-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.
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-R02 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R02 OCA].
+</div>
+<div class="pdbe-citations 1r02" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-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:[http://www.ncbi.nlm.nih.gov/pubmed/15479620 15479620]
+*[[Orexin and Orexin receptor|Orexin and Orexin receptor]]
-[[Category: Single protein]]
+== References ==
-[[Category: Hong, E.]]
+<references/>
-[[Category: Kim, H Y.]]
+__TOC__
-[[Category: Kim, J I.]]
+</StructureSection>
-[[Category: Lee, W.]]
+[[Category: Homo sapiens]]
-[[Category: Helix-loop-helix]]
+[[Category: Large Structures]]
-[[Category: Turn]]
+[[Category: Hong E]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 06:54:39 2008''
+[[Category: Kim H-Y]]
+[[Category: Kim J-I]]
+[[Category: Lee W]]