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1ioj
From Proteopedia
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| - | [[Image:1ioj.gif|left|200px]] | + | [[Image:1ioj.gif|left|200px]] |
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| - | '''HUMAN APOLIPOPROTEIN C-I, NMR, 18 STRUCTURES''' | + | {{Structure |
| + | |PDB= 1ioj |SIZE=350|CAPTION= <scene name='initialview01'>1ioj</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''HUMAN APOLIPOPROTEIN C-I, NMR, 18 STRUCTURES''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1IOJ is a [ | + | 1IOJ 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=1IOJ OCA]. |
==Reference== | ==Reference== | ||
| - | Sequence-specific 1H NMR resonance assignments and secondary structure of human apolipoprotein C-I in the presence of sodium dodecyl sulfate., Rozek A, Sparrow JT, Weisgraber KH, Cushley RJ, Biochem Cell Biol. 1998;76(2-3):267-75. PMID:[http:// | + | Sequence-specific 1H NMR resonance assignments and secondary structure of human apolipoprotein C-I in the presence of sodium dodecyl sulfate., Rozek A, Sparrow JT, Weisgraber KH, Cushley RJ, Biochem Cell Biol. 1998;76(2-3):267-75. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9923695 9923695] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: lipid association]] | [[Category: lipid association]] | ||
| - | ''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 11:52:56 2008'' |
Revision as of 09:52, 20 March 2008
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HUMAN APOLIPOPROTEIN C-I, NMR, 18 STRUCTURES
Overview
Apolipoprotein (apo) C-I is a 57-residue exchangeable plasma protein distributed mainly in high and very low density lipoprotein. In this report we present the nuclear magnetic resonance spectra of native apoC-I and synthetic apoC-I, containing selected 15N-labelled amino acids, in the presence of sodium dodecyl sulfate. The proton resonances of apoC-I are assigned and the secondary structure is estimated from the difference of measured alpha-proton chemical shifts to random coil values and the observed NOE interactions. According to these data apoC-I forms two helices, Val-4-Lys-30 and Leu-34-Lys-52, linked by an unstructured region Gln-31-Glu-33. The N-terminal segments of each helix, Val-4-Gly-15 and Leu-34-Met-38, appear to be more flexible than the helical core regions Asn-16-Lys-30 and Arg-39-Lys-52.
About this Structure
1IOJ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Sequence-specific 1H NMR resonance assignments and secondary structure of human apolipoprotein C-I in the presence of sodium dodecyl sulfate., Rozek A, Sparrow JT, Weisgraber KH, Cushley RJ, Biochem Cell Biol. 1998;76(2-3):267-75. PMID:9923695
Page seeded by OCA on Thu Mar 20 11:52:56 2008
