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1ya9

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Revision as of 06:07, 28 April 2021

Crystal Structure of the 22kDa N-Terminal Fragment of Mouse Apolipoprotein E

Structural highlights

1ya9 is a 1 chain structure with sequence from Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	Apoe (LK3 transgenic mice)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[APOE_MOUSE] Mediates the binding, internalization, and catabolism of lipoprotein particles. It can serve as a ligand for the LDL (apo B/E) receptor and for the specific apo-E receptor (chylomicron remnant) of hepatic tissues.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Apolipoprotein (apo) E4 is a major risk factor for Alzheimer and cardiovascular diseases. ApoE4 differs from the two other common isoforms (apoE2 and apoE3) by its lower resistance to denaturation and greater propensity to form partially folded intermediates. As a first step to determine the importance of stability differences in vivo, we reengineered a partially humanized variant of the amino-terminal domain of mouse apoE (T61R mouse apoE) to acquire a destabilized conformation like that of apoE4. For this process, we determined the crystal structure of wild-type mouse apoE, which, like apoE4, forms a four-helix bundle, and identified two structural differences in the turn between helices 2 and 3 and in the middle of helix 3 as potentially destabilizing sites. Introducing mutations G83T and N113G at these sites destabilized the mouse apoE conformation. The mutant mouse apoE more rapidly remodeled phospholipid than T61R mouse apoE, which supports the hypothesis that a destabilized conformation promotes apoE4 lipid binding.

Engineering conformational destabilization into mouse apolipoprotein E. A model for a unique property of human apolipoprotein E4.,Hatters DM, Peters-Libeu CA, Weisgraber KH J Biol Chem. 2005 Jul 15;280(28):26477-82. Epub 2005 May 11. PMID:15890642^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Hatters DM, Peters-Libeu CA, Weisgraber KH. Engineering conformational destabilization into mouse apolipoprotein E. A model for a unique property of human apolipoprotein E4. J Biol Chem. 2005 Jul 15;280(28):26477-82. Epub 2005 May 11. PMID:15890642 doi:10.1074/jbc.M503910200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ya9"

@@ Line 3: / Line 3: @@
 <StructureSection load='1ya9' size='340' side='right'caption='[[1ya9]], [[Resolution|resolution]] 2.09&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ya9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YA9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1YA9 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ya9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YA9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YA9 FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Apoe ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Apoe ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ya9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ya9 OCA], [http://pdbe.org/1ya9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ya9 RCSB], [http://www.ebi.ac.uk/pdbsum/1ya9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ya9 ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ya9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ya9 OCA], [https://pdbe.org/1ya9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ya9 RCSB], [https://www.ebi.ac.uk/pdbsum/1ya9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ya9 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/APOE_MOUSE APOE_MOUSE]] Mediates the binding, internalization, and catabolism of lipoprotein particles. It can serve as a ligand for the LDL (apo B/E) receptor and for the specific apo-E receptor (chylomicron remnant) of hepatic tissues.
+[[https://www.uniprot.org/uniprot/APOE_MOUSE APOE_MOUSE]] Mediates the binding, internalization, and catabolism of lipoprotein particles. It can serve as a ligand for the LDL (apo B/E) receptor and for the specific apo-E receptor (chylomicron remnant) of hepatic tissues.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1ya9

From Proteopedia

Revision as of 06:07, 28 April 2021

Crystal Structure of the 22kDa N-Terminal Fragment of Mouse Apolipoprotein E

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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