1r02

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[[Image:1r02.gif|left|200px]]
[[Image:1r02.gif|left|200px]]
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{{Structure
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|PDB= 1r02 |SIZE=350|CAPTION= <scene name='initialview01'>1r02</scene>
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The line below this paragraph, containing "STRUCTURE_1r02", creates the "Structure Box" on the page.
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{{STRUCTURE_1r02| PDB=1r02 | SCENE= }}
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|RELATEDENTRY=[[1cq0|1CQ0]]
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|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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'''Solution structure of Human Orexin-A:Regulator of Appetite and Wakefulness'''
'''Solution structure of Human Orexin-A:Regulator of Appetite and Wakefulness'''
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==About this Structure==
==About this Structure==
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1R02 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R02 OCA].
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1R02 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R02 OCA].
==Reference==
==Reference==
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[[Category: Kim, J I.]]
[[Category: Kim, J I.]]
[[Category: Lee, W.]]
[[Category: Lee, W.]]
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[[Category: helix-loop-helix]]
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[[Category: Helix-loop-helix]]
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[[Category: turn]]
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[[Category: Turn]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:54:39 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:21:19 2008''
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Revision as of 03:54, 3 May 2008

Image:1r02.gif

Template:STRUCTURE 1r02

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


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.

About this Structure

1R02 is a Single protein structure. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Sat May 3 06:54:39 2008

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