1nfo
From Proteopedia
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[[Image:1nfo.gif|left|200px]] | [[Image:1nfo.gif|left|200px]] | ||
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'''APOLIPOPROTEIN E2 (APOE2, D154A MUTATION)''' | '''APOLIPOPROTEIN E2 (APOE2, D154A MUTATION)''' | ||
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[[Category: Parkin, S.]] | [[Category: Parkin, S.]] | ||
[[Category: Rupp, B.]] | [[Category: Rupp, B.]] | ||
| - | [[Category: | + | [[Category: Hdl]] |
| - | [[Category: | + | [[Category: Heparin-binding]] |
| - | [[Category: | + | [[Category: Lipid transport]] |
| - | [[Category: | + | [[Category: Plasma protein]] |
| - | [[Category: | + | [[Category: Vldl]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:28:34 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 23:28, 2 May 2008
APOLIPOPROTEIN E2 (APOE2, D154A MUTATION)
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.
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 Page seeded by OCA on Sat May 3 02:28:34 2008
