1ron: Difference between revisions
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[[Image:1ron.gif|left|200px]] | [[Image:1ron.gif|left|200px]] | ||
'''NMR SOLUTION STRUCTURE OF HUMAN NEUROPEPTIDE Y''' | {{Structure | ||
|PDB= 1ron |SIZE=350|CAPTION= <scene name='initialview01'>1ron</scene> | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''NMR SOLUTION STRUCTURE OF HUMAN NEUROPEPTIDE Y''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1RON is a [ | 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]. | ||
==Reference== | ==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:[http:// | 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] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: NH2]] | [[Category: NH2]] | ||
[[Category: amidation]] | [[Category: amidation]] | ||
[[Category: cleavage on pair of basic | [[Category: cleavage on pair of basic residue]] | ||
[[Category: neuromodulator]] | [[Category: neuromodulator]] | ||
[[Category: neuropeptide]] | [[Category: neuropeptide]] | ||
[[Category: signal]] | [[Category: signal]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:54:16 2008'' | ||
Revision as of 11:54, 20 March 2008
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| Ligands: | NH2 | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
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].
Disease
Known diseases associated with this structure: Myelokathexis, isolated OMIM:[162643], WHIM syndrome OMIM:[162643]
About this Structure
1RON is a Single protein structure of sequence from Homo sapiens. Full crystallographic 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
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