1ron: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
New page: left|200px<br /> <applet load="1ron" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ron" /> '''NMR SOLUTION STRUCTURE OF HUMAN NEUROPEPTID...
 
No edit summary
 
(15 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1ron.gif|left|200px]]<br />
<applet load="1ron" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1ron" />
'''NMR SOLUTION STRUCTURE OF HUMAN NEUROPEPTIDE Y'''<br />


==Overview==
==NMR SOLUTION STRUCTURE OF HUMAN NEUROPEPTIDE Y==
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].
<StructureSection load='1ron' size='340' side='right'caption='[[1ron]]' scene=''>
 
== Structural highlights ==
==Disease==
<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>
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]]
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
 
<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>
==About this Structure==
<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>
1RON is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NH2 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1RON OCA].  
</table>
 
== Function ==
==Reference==
[https://www.uniprot.org/uniprot/NPY_HUMAN NPY_HUMAN] NPY is implicated in the control of feeding and in secretion of gonadotrophin-release hormone.
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://ispc.weizmann.ac.il//pmbin/getpm?pmid=9008359 9008359]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ro/1ron_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </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/main_output.php?pdb_ID=1ron ConSurf].
<div style="clear:both"></div>
__TOC__
</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 residues]]
[[Category: neuromodulator]]
[[Category: neuropeptide]]
[[Category: signal]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:06:01 2007''

Latest revision as of 11:25, 1 May 2024

NMR SOLUTION STRUCTURE OF HUMAN NEUROPEPTIDE YNMR SOLUTION STRUCTURE OF HUMAN NEUROPEPTIDE Y

Structural highlights

1ron is a 1 chain structure with sequence from Homo sapiens. The May 2012 RCSB PDB Molecule of the Month feature on Leptin by David Goodsell is 10.2210/rcsb_pdb/mom_2012_5. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
Retrieved from "https://proteopedia.openfox.io/wiki/index.php?title=1ron&oldid=4139983"