1ron
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(New page: 200px<br /> <applet load="1ron" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ron" /> '''NMR SOLUTION STRUCTURE OF HUMAN NEUROPEPTID...)
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Revision as of 16:59, 12 November 2007
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NMR SOLUTION STRUCTURE OF HUMAN NEUROPEPTIDE Y
Contents |
Overview
The three-dimensional structure of synthetic human neuropeptide Y in, aqueous solution at pH 3.2 and 37 degrees C was determined from, two-dimensional 1H NMR data recorded at 600 MHz. A restraint set, consisting of 440 interproton distance restraints inferred from NOEs and, 11 backbone and 4 side-chain dihedral angle restraints derived from, spin-spin coupling constants was used as input for distance geometry, calculations on DIANA and simulated annealing and restrained energy, minimization in X-PLOR. The final set of 26 structures is well defined in, the region of residues 11-36, with a mean pairwise rmsd of 0.51 A for the, backbone heavy atoms (N, C alpha and C) and 1.34 A for all heavy atoms., Residues 13-36 form an amphipathic alpha-helix. The N-terminal 10 residues, are poorly defined relative to the helical region, although some elements, of local structure are apparent. At least one of the three prolines in the, N-terminal region co-exists in both cis and trans conformations. An, additional set of 24 distances was interpreted as intermolecular distances, within a dimer. A combination of distance geometry and restrained, simulated annealing yielded a model of the dimer having antiparallel, packing of two helical units, whose hydrophobic faces form a well-defined, core. Sedimentation equilibrium experiments confirm the observation that, neuropeptide Y associates to form dimers and higher aggregates under the, conditions of the NMR experiments. Our results therefore support the, structural features reported for porcine neuropeptide Y [Cowley, D.J. et, al. (1992) Eur. J. Biochem., 205, 1099-1106] rather than the 'aPP' fold, described previously for human neuropeptide Y [Darbon, H. et al. (1992), Eur. J. Biochem., 209, 765-771].
Disease
Known diseases associated with this structure: Myelokathexis, isolated OMIM:[162643], WHIM syndrome OMIM:[162643]
About this Structure
1RON is a Single protein structure of sequence from Homo sapiens with NH2 as ligand. Full crystallographic information is available from OCA.
Reference
Solution structure of human neuropeptide Y., Monks SA, Karagianis G, Howlett GJ, Norton RS, J Biomol NMR. 1996 Dec;8(4):379-90. PMID:9008359
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