1nfo
From Proteopedia
(New page: 200px<br /> <applet load="1nfo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nfo, resolution 2.0Å" /> '''APOLIPOPROTEIN E2 (A...) |
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| - | [[Image:1nfo.gif|left|200px]]<br /> | + | [[Image:1nfo.gif|left|200px]]<br /><applet load="1nfo" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1nfo" size=" | + | |
caption="1nfo, resolution 2.0Å" /> | caption="1nfo, resolution 2.0Å" /> | ||
'''APOLIPOPROTEIN E2 (APOE2, D154A MUTATION)'''<br /> | '''APOLIPOPROTEIN E2 (APOE2, D154A MUTATION)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The defective binding of apolipoprotein (apo) E2 to lipoprotein receptors, an underlying cause of type III hyperlipoproteinemia, results from | + | The defective binding of apolipoprotein (apo) E2 to lipoprotein receptors, an underlying cause of type III hyperlipoproteinemia, results from replacement of Arg 158 with Cys, disrupting the naturally occurring salt bridge between Asp 154 and Arg 158. A new bond between Asp 154 and Arg 150 is formed, shifting Arg 150 out of the receptor binding region. Elimination of the 154-150 salt bridge by site-directed mutagenesis of Asp 154 to Ala restored the receptor binding activity to near normal levels. The X-ray crystal structure of apoE2 Ala 154 demonstrated that Arg 150 was relocated within the receptor binding region. Our results demonstrate that defective binding of apoE2 occurs by a novel mechanism of the replacement of one salt bridge with another. |
==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== | ||
| - | 1NFO 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:// | + | 1NFO 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=1NFO 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 Thu Feb 21 14:05:32 2008'' |
Revision as of 12:05, 21 February 2008
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APOLIPOPROTEIN E2 (APOE2, D154A MUTATION)
Contents |
Overview
The defective binding of apolipoprotein (apo) E2 to lipoprotein receptors, an underlying cause of type III hyperlipoproteinemia, results from replacement of Arg 158 with Cys, disrupting the naturally occurring salt bridge between Asp 154 and Arg 158. A new bond between Asp 154 and Arg 150 is formed, shifting Arg 150 out of the receptor binding region. Elimination of the 154-150 salt bridge by site-directed mutagenesis of Asp 154 to Ala restored the receptor binding activity to near normal levels. The X-ray crystal structure of apoE2 Ala 154 demonstrated that Arg 150 was relocated within the receptor binding region. Our results demonstrate that defective binding of apoE2 occurs by a novel mechanism of the replacement of one salt bridge with another.
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
1NFO is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Novel mechanism for defective receptor binding of apolipoprotein E2 in type III hyperlipoproteinemia., Dong LM, Parkin S, Trakhanov SD, Rupp B, Simmons T, Arnold KS, Newhouse YM, Innerarity TL, Weisgraber KH, Nat Struct Biol. 1996 Aug;3(8):718-22. PMID:8756331
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