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[[Image:1ron.gif|left|200px]]


{{Structure
==NMR SOLUTION STRUCTURE OF HUMAN NEUROPEPTIDE Y==
|PDB= 1ron |SIZE=350|CAPTION= <scene name='initialview01'>1ron</scene>
<StructureSection load='1ron' size='340' side='right'caption='[[1ron]]' scene=''>
|SITE=
== Structural highlights ==
|LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene>
<table><tr><td colspan='2'>[[1ron]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. 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>
|ACTIVITY=  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
|GENE=
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[https://proteopedia.org/fgij/fg.htm?mol=1ron FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ron OCA], [https://pdbe.org/1ron PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ron RCSB], [https://www.ebi.ac.uk/pdbsum/1ron PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ron ProSAT]</span></td></tr>
 
</table>
'''NMR SOLUTION STRUCTURE OF HUMAN NEUROPEPTIDE Y'''
== Function ==
 
[https://www.uniprot.org/uniprot/NPY_HUMAN NPY_HUMAN] NPY is implicated in the control of feeding and in secretion of gonadotrophin-release hormone.
 
== Evolutionary Conservation ==
==Overview==
[[Image:Consurf_key_small.gif|200px|right]]
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].
Check<jmol>
 
  <jmolCheckbox>
==Disease==
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ro/1ron_consurf.spt"</scriptWhenChecked>
Known diseases associated with this structure: Myelokathexis, isolated OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=162643 162643]], WHIM syndrome OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=162643 162643]]
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 
    <text>to colour the structure by Evolutionary Conservation</text>
==About this Structure==
  </jmolCheckbox>
1RON is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RON OCA].  
</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>
==Reference==
__TOC__
Solution structure of human neuropeptide Y., Monks SA, Karagianis G, Howlett GJ, Norton RS, J Biomol NMR. 1996 Dec;8(4):379-90. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9008359 9008359]
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Howlett, G J.]]
[[Category: Leptin]]
[[Category: Karagianis, G.]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Monks, S A.]]
[[Category: Howlett GJ]]
[[Category: Norton, R S.]]
[[Category: Karagianis G]]
[[Category: NH2]]
[[Category: Monks SA]]
[[Category: amidation]]
[[Category: Norton RS]]
[[Category: cleavage on pair of basic residue]]
[[Category: neuromodulator]]
[[Category: neuropeptide]]
[[Category: signal]]
 
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Latest revision as of 08:25, 1 May 2024

NMR SOLUTION STRUCTURE OF HUMAN NEUROPEPTIDE Y

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