A complete NMR spectral assignment of the lipid-free mouse apolipoprotein A-I (apoAI) C-terminal truncation mutant, apoAI(1-216)
ApoAI is the major protein component of the high-density lipoprotein (HDL) that has been a hot subject of interests because of its anti-atherogenic properties. Lipid-free apoAI specifically binds to phospholipids, triggering HDL formation. Here we report a complete backbone assignment and nearly com...
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| Published in | Biomolecular NMR assignments Vol. 1; no. 1; pp. 109 - 111 |
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| Main Authors | , , |
| Format | Journal Article |
| Language | English |
| Published |
Netherlands
Springer Nature B.V
01.07.2007
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| Online Access | Get full text |
| ISSN | 1874-2718 1874-270X 1874-270X |
| DOI | 10.1007/s12104-007-9031-2 |
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| Abstract | ApoAI is the major protein component of the high-density lipoprotein (HDL) that has been a hot subject of interests because of its anti-atherogenic properties. Lipid-free apoAI specifically binds to phospholipids, triggering HDL formation. Here we report a complete backbone assignment and nearly complete sidechain assignment of a C-terminal 24-residue truncation mutant of mouse apoAI, apoAI(1-216), in its lipid-free form. |
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| AbstractList | ApoAI is the major protein component of the high-density lipoprotein (HDL) that has been a hot subject of interests because of its anti-atherogenic properties. Lipid-free apoAI specifically binds to phospholipids, triggering HDL formation. Here we report a complete backbone assignment and nearly complete sidechain assignment of a C-terminal 24-residue truncation mutant of mouse apoAI, apoAI(1-216), in its lipid-free form. ApoAI is the major protein component of the high-density lipoprotein (HDL) that has been a hot subject of interests because of its anti-atherogenic properties. Lipid-free apoAI specifically binds to phospholipids, triggering HDL formation. Here we report a complete backbone assignment and nearly complete sidechain assignment of a C-terminal 24-residue truncation mutant of mouse apoAI, apoAI(1-216), in its lipid-free form.ApoAI is the major protein component of the high-density lipoprotein (HDL) that has been a hot subject of interests because of its anti-atherogenic properties. Lipid-free apoAI specifically binds to phospholipids, triggering HDL formation. Here we report a complete backbone assignment and nearly complete sidechain assignment of a C-terminal 24-residue truncation mutant of mouse apoAI, apoAI(1-216), in its lipid-free form. ApoAI is the major protein component of the high-density lipoprotein (HDL) that has been a hot subject of interests because of its anti-atherogenic properties. Lipid-free apoAI specifically binds to phospholipids, triggering HDL formation. Here we report a complete backbone assignment and nearly complete sidechain assignment of a C-terminal 24-residue truncation mutant of mouse apoAI, apoAI(1-216), in its lipid-free form.[PUBLICATION ABSTRACT] |
| Author | Wang, Jianjun Yang, Yunhuang Hoyt, David |
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| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/19636841$$D View this record in MEDLINE/PubMed |
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| Cites_doi | 10.1161/01.ATV.0000104029.74961.f5 10.1038/365762a0 10.1016/S0021-9258(17)33810-3 10.1016/S1388-1981(01)00081-6 10.1074/jbc.M107883200 10.1021/ja00093a069 10.1073/pnas.0506877103 10.1007/BF00404272 10.1007/BF00197809 10.1021/bi0508385 |
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| SubjectTerms | Animals Apolipoprotein A-I - chemistry Apolipoprotein A-I - genetics Lipids Lipids - chemistry Low density lipoprotein Mice Molecular Structure Nuclear Magnetic Resonance, Biomolecular Peptide Fragments - chemistry Peptide Fragments - genetics Protein Structure, Secondary Recombinant Proteins - chemistry Recombinant Proteins - genetics Sequence Deletion |
| Title | A complete NMR spectral assignment of the lipid-free mouse apolipoprotein A-I (apoAI) C-terminal truncation mutant, apoAI(1-216) |
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