1R02

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

Summary for 1R02

• Entry DOI: 10.2210/pdb1r02/pdb
• Related: 1CQ0
• NMR Information: BMRB: 5994
• Descriptor: Orexin-A (1 entity in total)
• Functional Keywords: turn, helix-loop-helix, neuropeptide
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 3588.19

Authors

Kim, H.-Y.,Hong, E.,Kim, J.-I.,Lee, W. (deposition date: 2003-09-19, release date: 2004-09-19, Last modification date: 2024-10-23)

Primary citation

Kim, H.Y.,Hong, E.,Kim, J.I.,Lee, W.
Solution structure of human orexin-A: regulator of appetite and wakefulness.
J.Biochem.Mol.Biol., 37:565-573, 2004

PubMed Abstract: 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.

PubMed: 15479620
DOI: 10.5483/BMBRep.2004.37.5.565

Experimental method

SOLUTION NMR