View source for 3wsy


==SorLA Vps10p domain in complex with its own propeptide fragment==
<StructureSection load='3wsy' size='340' side='right'caption='[[3wsy]], [[Resolution|resolution]] 3.11&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3wsy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WSY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WSY FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.11&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=3wsy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wsy OCA], [https://pdbe.org/3wsy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wsy RCSB], [https://www.ebi.ac.uk/pdbsum/3wsy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wsy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SORL_HUMAN SORL_HUMAN] Likely to be a multifunctional endocytic receptor, that may be implicated in the uptake of lipoproteins and of proteases. Binds LDL, the major cholesterol-carrying lipoprotein of plasma, and transports it into cells by endocytosis. Binds the receptor-associated protein (RAP). Could play a role in cell-cell interaction.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
SorLA is a neuronal sorting receptor considered to be a major risk factor for Alzheimer's disease. We have recently reported that it directs lysosomal targeting of nascent neurotoxic amyloid-beta (Abeta) peptides by directly binding Abeta. Here, we determined the crystal structure of the human sorLA domain responsible for Abeta capture, Vps10p, in an unbound state and in complex with two ligands. Vps10p assumes a ten-bladed beta-propeller fold with a large tunnel at the center. An internal ligand derived from the sorLA propeptide bound inside the tunnel to extend the beta-sheet of one of the propeller blades. The structure of the sorLA Vps10p-Abeta complex revealed that the same site is used. Peptides are recognized by sorLA Vps10p in redundant modes without strict dependence on a particular amino acid sequence, thus suggesting a broad specificity toward peptides with a propensity for beta-sheet formation.

Structural basis for amyloidogenic peptide recognition by sorLA.,Kitago Y, Nagae M, Nakata Z, Yagi-Utsumi M, Takagi-Niidome S, Mihara E, Nogi T, Kato K, Takagi J Nat Struct Mol Biol. 2015 Mar;22(3):199-206. doi: 10.1038/nsmb.2954. Epub 2015, Feb 2. PMID:25643321<ref>PMID:25643321</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3wsy" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Kitago Y]]
[[Category: Nagae M]]
[[Category: Nakata Z]]
[[Category: Nogi T]]
[[Category: Takagi J]]