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| | {{STRUCTURE_2fq8| PDB=2fq8 | SCENE= }} | | {{STRUCTURE_2fq8| PDB=2fq8 | SCENE= }} |
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| - | '''NMR structure of 2F associated with lipid disc'''
| + | ===NMR structure of 2F associated with lipid disc=== |
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| - | ==Overview==
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| - | Class A amphipathic helical peptides have been shown to mimic apolipoprotein A-I, the major protein component of high density lipoproteins and have been shown to inhibit atherosclerosis in several dyslipidemic mouse models. Previously we reported the NMR structure of Ac-18A-NH2, the base-line model class A amphipathic helical peptide in a 50% (v/v) trifluoroethanol-d3/water mixture, a membrane-mimic environment (Mishra, V. K., Palgunachari, M. N., Anantharamaiah, G. M., Jones, M. K., Segrest, J. P., and Krishna, N. R. (2001) Peptides 22, 567-573). The peptide Ac-18A-NH2 forms discoidal nascent high density lipoprotein-like particles with 1,2-dimyristoyl-sn-glycero-3-phosphocholine. Because subtle structural changes in the peptide.lipid complexes have been shown to be responsible for their antiatherogenic properties, we undertook high resolution NMR studies to deduce detailed structure of recombinant peptide.1,2-dimyristoyl-sn-glycero-3-phosphocholine complexes. The peptide adopts a well defined amphipathic alpha helical structure in association with the lipid at a 1:1 peptide:lipid weight ratio. Nuclear Overhauser effect spectroscopy revealed a number of intermolecular close contacts between the aromatic residues in the hydrophobic face of the helix and the lipid acyl chain protons. The pattern of observed peptide-lipid nuclear Overhauser effects is consistent with a parallel orientation of the amphipathic alpha helix, with respect to the plane of the lipid bilayer, on the edge of the disc (the belt model). Based on the results of chemical cross-linking and molecular modeling, we propose that peptide helices are arranged in a head to tail fashion to cover the edge of the disc. This arrangement of peptides is also consistent with the pKa values of the Lys residues determined previously. Taken together, these results provide for the first time a high resolution structural view of the peptide.lipid discoidal complexes formed by a class A amphipathic alpha helical peptide.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16407255}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16407255 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16407255}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FQ8 OCA]. | + | Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FQ8 OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Amphipathic helix]] | | [[Category: Amphipathic helix]] |
| | [[Category: Class a helix]] | | [[Category: Class a helix]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:11:41 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 12:37:21 2008'' |
Revision as of 09:37, 27 July 2008
Template:STRUCTURE 2fq8
NMR structure of 2F associated with lipid disc
Template:ABSTRACT PUBMED 16407255
About this Structure
Full experimental information is available from OCA.
Reference
Association of a model class A (apolipoprotein) amphipathic alpha helical peptide with lipid: high resolution NMR studies of peptide.lipid discoidal complexes., Mishra VK, Anantharamaiah GM, Segrest JP, Palgunachari MN, Chaddha M, Sham SW, Krishna NR, J Biol Chem. 2006 Mar 10;281(10):6511-9. Epub 2006 Jan 9. PMID:16407255
Page seeded by OCA on Sun Jul 27 12:37:21 2008
