7vt0
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Dimer structure of SORLA== | |
| + | <StructureSection load='7vt0' size='340' side='right'caption='[[7vt0]], [[Resolution|resolution]] 3.40Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[7vt0]] 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=7VT0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7VT0 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.4Å</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=7vt0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7vt0 OCA], [https://pdbe.org/7vt0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7vt0 RCSB], [https://www.ebi.ac.uk/pdbsum/7vt0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7vt0 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 == | ||
| + | Sorting-related receptor with A-type repeats (SORLA) is an important receptor for regulating normal cellular functions via protein sorting. Here, we determined the structures of the full-length SORLA and identified two distinct conformations of apo-SORLA using single-particle cryogenic electron microscopy. In contrast to homologous proteins, both monomer and dimer forms of SORLA existed in a neutral solution. Only three hydrogen bonds in the vicinity of the dimer interface implied the involvement in dimerization. The orientation of residue R490 was a key point for ligand binding. These results suggest a unique mechanism of SORLA dimerization for protein trafficking. | ||
| - | + | Cryo-EM structures reveal distinct apo conformations of sortilin-related receptor SORLA.,Zhang X, Wu C, Song Z, Sun D, Zhai L, Liu C Biochem Biophys Res Commun. 2022 Apr 16;600:75-79. doi: , 10.1016/j.bbrc.2022.01.108. Epub 2022 Feb 12. PMID:35196630<ref>PMID:35196630</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 7vt0" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Cang W]] | ||
| + | [[Category: Chuang L]] | ||
| + | [[Category: Xi Z]] | ||
Current revision
Dimer structure of SORLA
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Categories: Homo sapiens | Large Structures | Cang W | Chuang L | Xi Z
