1r02: Difference between revisions
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|ACTIVITY= | |ACTIVITY= | ||
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|RELATEDENTRY=[[1cq0|1CQ0]] | |||
|RESOURCES=<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.ebi.ac.uk/pdbsum/1r02 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1r02 RCSB]</span> | |||
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==Overview== | ==Overview== | ||
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. | 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== | ==About this Structure== | ||
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[[Category: turn]] | [[Category: turn]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:21:19 2008'' | ||
Revision as of 23:21, 30 March 2008
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| Related: | 1CQ0
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution structure of Human Orexin-A:Regulator of Appetite and Wakefulness
OverviewOverview
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 StructureAbout this Structure
1R02 is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
ReferenceReference
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
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