1ron

<StructureSection load='1ron' size='340' side='right'caption='[[1ron]], [[NMR_Ensembles_of_Models | 26 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1ron]] is a 1 chain structure. The May 2012 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Leptin'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2012_5 10.2210/rcsb_pdb/mom_2012_5]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RON OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RON FirstGlance]. <br>

</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>

[[https://www.uniprot.org/uniprot/NPY_HUMAN NPY_HUMAN]] NPY is implicated in the control of feeding and in secretion of gonadotrophin-release hormone.

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== Publication Abstract from PubMed ==

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].

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<ref>PMID:9008359</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1ron" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Howlett, G J]]

[[Category: Karagianis, G]]

[[Category: Monks, S A]]

[[Category: Norton, R S]]

[[Category: Neuropeptide]]