1CQ0
SOLUTION STRUCTURE OF A HUMAN HYPOCRETIN-2/OREXIN-B'SOLUTION STRUCTURE OF A HUMAN HYPOCRETIN-2/OREXIN-B '
Summary for 1CQ0
| Entry DOI | 10.2210/pdb1cq0/pdb |
| Descriptor | PROTEIN (NEW HYPOTHALAMIC NEUROPEPTIDE/OREXIN-B28) (1 entity in total) |
| Functional Keywords | obesity, human hcrt-2/ox-b, neuropeptide, solution structure, de novo protein |
| Biological source | Homo sapiens (human) |
| Cellular location | Rough endoplasmic reticulum : O43612 |
| Total number of polymer chains | 1 |
| Total formula weight | 2894.34 |
| 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 citation | Lee, 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: 10583376DOI: 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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