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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
25
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pubmed:dateCreated |
2002-12-11
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pubmed:abstractText |
Serum amyloid A (SAA) is a small apolipoprotein that binds to high-density lipoproteins in the serum. Although SAA seems to play a role in host defense and lipid transport and metabolism, its specific functions have not been defined. Despite the growing implications that SAA plays a role in the pathology of various diseases, a high-resolution structure of SAA is lacking because of limited solubility in the high-density lipoprotein-free form. In this study, complementary methods including glutaraldehyde cross-linking, size-exclusion chromatography, and sedimentation-velocity analytical ultracentrifugation were used to show that murine SAA2.2 in aqueous solution exists in a monomer-hexamer equilibrium. Electron microscopy of hexameric SAA2.2 revealed that the subunits are arranged in a ring forming a putative central channel. Limited trypsin proteolysis and mass spectrometry analysis identified a significantly protease-resistant SAA2.2 region comprising residues 39-86. The isolated 39-86 SAA2.2 fragment did not hexamerize, suggesting that part of the N terminus is involved in SAA2.2 hexamer formation. Circular-dichroism spectrum deconvolution and secondary-structure prediction suggest that SAA2.2 contains approximately 50% of its residues in alpha-helical conformation and <10% in beta-structure. These findings are consistent with the recent discovery that human SAA1.1 forms a membrane channel and have important implications for understanding the 3D structure, multiple functions, and pathological roles of this highly conserved protein.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/12456883-10066777,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12456883-10211414,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12456883-10504381,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12456883-10608507,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12456883-11112271,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12456883-11140693,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12456883-11454373,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12456883-11830469,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12456883-12000193,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12456883-12021428,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12456883-12124613,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12456883-1731787,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12456883-198813,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12456883-2835617,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12456883-3223951,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12456883-3561251,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12456883-3707915,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12456883-3922050,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12456883-3950541,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12456883-5700707,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12456883-6411718,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12456883-6693836,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12456883-7172504,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12456883-7769239,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12456883-7827140,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12456883-7901995,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12456883-8054364,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12456883-8188253,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12456883-8376413,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12456883-8742743,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12456883-8743704,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12456883-8836154,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12456883-8906588,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12456883-8994630,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12456883-9743207,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12456883-9767146,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12456883-978136,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12456883-9822267,
http://linkedlifedata.com/resource/pubmed/commentcorrection/12456883-9931277
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
99
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
15947-52
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:12456883-Amyloidosis,
pubmed-meshheading:12456883-Animals,
pubmed-meshheading:12456883-Biopolymers,
pubmed-meshheading:12456883-Chromatography, Gel,
pubmed-meshheading:12456883-Chromatography, High Pressure Liquid,
pubmed-meshheading:12456883-Circular Dichroism,
pubmed-meshheading:12456883-Cross-Linking Reagents,
pubmed-meshheading:12456883-Glutaral,
pubmed-meshheading:12456883-Mass Spectrometry,
pubmed-meshheading:12456883-Mice,
pubmed-meshheading:12456883-Microscopy, Electron,
pubmed-meshheading:12456883-Protein Structure, Secondary,
pubmed-meshheading:12456883-Recombinant Fusion Proteins,
pubmed-meshheading:12456883-Serum Amyloid A Protein,
pubmed-meshheading:12456883-Structure-Activity Relationship,
pubmed-meshheading:12456883-Trypsin,
pubmed-meshheading:12456883-Ultracentrifugation
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pubmed:year |
2002
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pubmed:articleTitle |
Murine apolipoprotein serum amyloid A in solution forms a hexamer containing a central channel.
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pubmed:affiliation |
Department of Chemistry, Rensselaer Polytechnic Institute, 110 8th Street, Troy, NY 12180, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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