1oef
From Proteopedia
(New page: 200px<br /> <applet load="1oef" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oef" /> '''PEPTIDE OF HUMAN APOE RESIDUES 263-286, NMR...) |
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'''PEPTIDE OF HUMAN APOE RESIDUES 263-286, NMR, 5 STRUCTURES AT PH 4.8, 37 DEGREES CELSIUS AND PEPTIDE:SDS MOLE RATIO OF 1:90'''<br /> | '''PEPTIDE OF HUMAN APOE RESIDUES 263-286, NMR, 5 STRUCTURES AT PH 4.8, 37 DEGREES CELSIUS AND PEPTIDE:SDS MOLE RATIO OF 1:90'''<br /> | ||
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==Disease== | ==Disease== | ||
| - | Known diseases associated with this structure: Alzheimer disease-2 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=107741 107741]], Hyperlipoproteinemia, type III OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=107741 107741]], Macular degeneration, age-related OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=107741 107741]], Myocardial infarction susceptibility OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=107741 107741]], Sea-blue histiocyte disease OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=107741 107741]] | + | Known diseases associated with this structure: Alzheimer disease-2 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=107741 107741]], Hyperlipoproteinemia, type III OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=107741 107741]], Lipoprotein glomerulopathy OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=107741 107741]], Macular degeneration, age-related OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=107741 107741]], Myocardial infarction susceptibility OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=107741 107741]], Sea-blue histiocyte disease OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=107741 107741]] |
==About this Structure== | ==About this Structure== | ||
| - | 1OEF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1OEF is a [http://en.wikipedia.org/wiki/Single_protein 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=1OEF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: vldl]] | [[Category: vldl]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:33:58 2008'' |
Revision as of 14:33, 15 February 2008
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PEPTIDE OF HUMAN APOE RESIDUES 263-286, NMR, 5 STRUCTURES AT PH 4.8, 37 DEGREES CELSIUS AND PEPTIDE:SDS MOLE RATIO OF 1:90
Contents |
Overview
Structures of apoE(263-286) and apoE(267-289) have been determined in, aqueous solution containing 90-fold molar excess of perdeuterated sodium, dodecyl sulfate by CD and 1H NMR. Conformations were calculated by, distance geometry based on 370 and 276 NOE distance restraints, respectively. RMSD for superimposing the region 265-284 from an ensemble, of 41 structures for apoE(263-286) is 0.64 +/- 0.17 A for backbone atoms, (N, C alpha, C = O) and 1.51 +/- 0.13 A for all atoms. The backbone RMSD, for an ensemble of 37 structures for apoE(267-289) is 0.74 +/- 0.21 A for, the region 268-275 and 0.34 +/- 0.10 A for the region 276-286. A, two-domain structure was found for apoE(267-289) with the C-terminal half, adopting a very well defined helix and the N-terminal segment 268-275 a, less well defined helix, suggesting that the N-terminus may weakly bind to, SDS. For apoE(263-286), an amphipathic helix-bend-helix structural motif, was found with all hydrophobic side chains on the concave face. The, existence of a bend around residues Q273 to G278 is consistent with their, temperature coefficients of amide protons as well as secondary shifts of, alpha-protons. Comparison of the structures of the two peptides revealed, that the enhanced binding of apoE(263-286) to lipid could be attributed to, the formation of a hydrophobic cluster consisting of residues W264, F265, L268, and V269. Aromatic side chains are proposed to be especially, important in anchoring apolipoprotein fragments to micelles.
Disease
Known diseases associated with this structure: Alzheimer disease-2 OMIM:[107741], Hyperlipoproteinemia, type III OMIM:[107741], Lipoprotein glomerulopathy OMIM:[107741], Macular degeneration, age-related OMIM:[107741], Myocardial infarction susceptibility OMIM:[107741], Sea-blue histiocyte disease OMIM:[107741]
About this Structure
1OEF is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Conformations of human apolipoprotein E(263-286) and E(267-289) in aqueous solutions of sodium dodecyl sulfate by CD and 1H NMR., Wang G, Pierens GK, Treleaven WD, Sparrow JT, Cushley RJ, Biochemistry. 1996 Aug 13;35(32):10358-66. PMID:8756691
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