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| | {{STRUCTURE_1ron| PDB=1ron | SCENE= }} | | {{STRUCTURE_1ron| PDB=1ron | SCENE= }} |
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| - | '''NMR SOLUTION STRUCTURE OF HUMAN NEUROPEPTIDE Y'''
| + | ===NMR SOLUTION STRUCTURE OF HUMAN NEUROPEPTIDE Y=== |
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| - | ==Overview==
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| - | 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. |
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| | + | {{ABSTRACT_PUBMED_9008359}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 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]. | + | 1RON 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]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Neuropeptide]] | | [[Category: Neuropeptide]] |
| | [[Category: Signal]] | | [[Category: Signal]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:44:02 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:46:10 2008'' |
Revision as of 23:46, 28 July 2008
Template:STRUCTURE 1ron
NMR SOLUTION STRUCTURE OF HUMAN NEUROPEPTIDE Y
Template:ABSTRACT PUBMED 9008359
About this Structure
1RON is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.
Reference
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
Page seeded by OCA on Tue Jul 29 02:46:10 2008
