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1r02

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Solution structure of Human Orexin-A:Regulator of Appetite and Wakefulness

Structural highlights

1r02 is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

OREX_HUMAN Defects in HCRT are the cause of narcolepsy type 1 (NRCLP1) [MIM: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.^[1]

Function

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.

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Peyron C, Faraco J, Rogers W, Ripley B, Overeem S, Charnay Y, Nevsimalova S, Aldrich M, Reynolds D, Albin R, Li R, Hungs M, Pedrazzoli M, Padigaru M, Kucherlapati M, Fan J, Maki R, Lammers GJ, Bouras C, Kucherlapati R, Nishino S, Mignot E. A mutation in a case of early onset narcolepsy and a generalized absence of hypocretin peptides in human narcoleptic brains. Nat Med. 2000 Sep;6(9):991-7. PMID:10973318 doi:10.1038/79690
↑ Kim HY, Hong E, Kim JI, Lee W. Solution structure of human orexin-A: regulator of appetite and wakefulness. J Biochem Mol Biol. 2004 Sep 30;37(5):565-73. PMID:15479620

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1r02"

@@ Line 1: / Line 1: @@
 ==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=''>
+<StructureSection load='1r02' size='340' side='right'caption='[[1r02]]' 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>
+<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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1cq0|1cq0]]</td></tr>
+</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>
-<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://pdbe.org/1r02 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1r02 RCSB], [http://www.ebi.ac.uk/pdbsum/1r02 PDBsum]</span></td></tr>
 </table>
 == 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>
+[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 ==
-[[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.
+[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 ==
@@ Line 19: / Line 19: @@
 </div>
 <div class="pdbe-citations 1r02" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Orexin and Orexin receptor|Orexin and Orexin receptor]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Hong, E]]
+[[Category: Homo sapiens]]
-[[Category: Kim, H Y]]
+[[Category: Large Structures]]
-[[Category: Kim, J I]]
+[[Category: Hong E]]
-[[Category: Lee, W]]
+[[Category: Kim H-Y]]
-[[Category: Helix-loop-helix]]
+[[Category: Kim J-I]]
-[[Category: Neuropeptide]]
+[[Category: Lee W]]
-[[Category: Turn]]

1r02

From Proteopedia

Current revision

Solution structure of Human Orexin-A:Regulator of Appetite and Wakefulness

Structural highlights

Disease

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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