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1CQ0

SOLUTION STRUCTURE OF A HUMAN HYPOCRETIN-2/OREXIN-B'SOLUTION STRUCTURE OF A HUMAN HYPOCRETIN-2/OREXIN-B '

Summary for 1CQ0
Entry DOI10.2210/pdb1cq0/pdb
DescriptorPROTEIN (NEW HYPOTHALAMIC NEUROPEPTIDE/OREXIN-B28) (1 entity in total)
Functional Keywordsobesity, human hcrt-2/ox-b, neuropeptide, solution structure, de novo protein
Biological sourceHomo sapiens (human)
Cellular locationRough endoplasmic reticulum : O43612
Total number of polymer chains1
Total formula weight2894.34
Authors
Lee, K.-H.,Bang, E.J.,Chae, K.-J.,Lee, D.W.,Lee, W. (deposition date: 1999-08-04, release date: 2000-01-10, Last modification date: 2024-04-10)
Primary citationLee, J.H.,Bang, E.,Chae, K.J.,Kim, J.Y.,Lee, D.W.,Lee, W.
Solution structure of a new hypothalamic neuropeptide, human hypocretin-2/orexin-B.
Eur.J.Biochem., 266:831-839, 1999
Cited by
PubMed Abstract: Orexin-A and orexin-B (also called hypocretin-1 and hypocretin-2, respectively) are novel hypothalamic neuropeptides encoded by a single mRNA transcript; they stimulate food intake. We have determined the three-dimensional solution structure of human hypocretin-2/orexin-B using two-dimensional 1H-NMR data and dynamical simulated annealing calculations. On the basis of NOEs, 3JHNalpha coupling constants and hydrogen-deuterium exchange rates together with chemical shift indices, human hypocretin-2/orexin-B was deduced to consist of two alpha-helices connected with a short linker in both H2O and 30% trifluoroethanol solutions. The helical axis of helix I is oriented about 60-80 degrees relative to helix II. Hybrid distance geometry and simulated-annealing protocols were used to generate an ensemble of 30 structures with no constraint violations greater than 0.03 nm for distances and 3 degrees for angles. In addition, human hypocretin-2/orexin-B shares a similar secondary-structural motif with human neuropeptide Y. This result can form the basis for further study on ligand-receptor recognition of human orexin receptors.
PubMed: 10583376
DOI: 10.1046/j.1432-1327.1999.00911.x
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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