1ioj
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
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| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ioj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ioj OCA], [http://www.ebi.ac.uk/pdbsum/1ioj PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ioj RCSB]</span> | ||
}} | }} | ||
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[[Category: lipid association]] | [[Category: lipid association]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:22:31 2008'' |
Revision as of 18:22, 30 March 2008
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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