7vt0: Difference between revisions

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'''Unreleased structure'''


The entry 7vt0 is ON HOLD
==Dimer structure of SORLA==
<StructureSection load='7vt0' size='340' side='right'caption='[[7vt0]], [[Resolution|resolution]] 3.40&Aring;' 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]] 3.4&#8491;</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.


Authors:  
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>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</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]]
Retrieved from "https://proteopedia.org/7vt0"