1ron: Difference between revisions
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==NMR SOLUTION STRUCTURE OF HUMAN NEUROPEPTIDE Y== | ==NMR SOLUTION STRUCTURE OF HUMAN NEUROPEPTIDE Y== | ||
<StructureSection load='1ron' size='340' side='right' caption='[[1ron]], [[NMR_Ensembles_of_Models | 26 NMR models]]' scene=''> | <StructureSection load='1ron' size='340' side='right' caption='[[1ron]], [[NMR_Ensembles_of_Models | 26 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ron]] is a 1 chain structure | <table><tr><td colspan='2'>[[1ron]] is a 1 chain structure. The May 2012 RCSB PDB [http://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 [http://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 [http://oca.weizmann.ac.il/oca-docs/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> | </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> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ron FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ron OCA], [http://pdbe.org/1ron PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ron RCSB], [http://www.ebi.ac.uk/pdbsum/1ron PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ron FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ron OCA], [http://pdbe.org/1ron PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ron RCSB], [http://www.ebi.ac.uk/pdbsum/1ron PDBsum]</span></td></tr> | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/ | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ron ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Leptin]] | [[Category: Leptin]] | ||
[[Category: RCSB PDB Molecule of the Month]] | [[Category: RCSB PDB Molecule of the Month]] | ||
Revision as of 11:25, 1 June 2016
NMR SOLUTION STRUCTURE OF HUMAN NEUROPEPTIDE YNMR SOLUTION STRUCTURE OF HUMAN NEUROPEPTIDE Y
Structural highlights
Function[NPY_HUMAN] NPY is implicated in the control of feeding and in secretion of gonadotrophin-release hormone. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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