1ron: Difference between revisions

Revision as of 02:46, 29 July 2008

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File:1ron.png

Template:STRUCTURE 1ron

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

Template:ABSTRACT PUBMED 9008359

About this StructureAbout this Structure

1RON is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

ReferenceReference

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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-[[Image:1ron.gif|left|200px]]
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 {{STRUCTURE_1ron|  PDB=1ron  |  SCENE=  }}
-'''NMR SOLUTION STRUCTURE OF HUMAN NEUROPEPTIDE Y'''
+===NMR SOLUTION STRUCTURE OF HUMAN NEUROPEPTIDE Y===
-==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].
+The line below this paragraph, {{ABSTRACT_PUBMED_9008359}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9008359 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9008359}}
 ==About this Structure==
-RON 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].
+RON is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RON OCA].
 ==Reference==
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 [[Category: Neuropeptide]]
 [[Category: Signal]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 07:44:02 2008''
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