View source for 8qvw


==Cryo-EM structure of the peptide binding domain of human SRP68/72==
<StructureSection load='8qvw' size='340' side='right'caption='[[8qvw]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8qvw]] 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=8QVW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8QVW 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&#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=8qvw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8qvw OCA], [https://pdbe.org/8qvw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8qvw RCSB], [https://www.ebi.ac.uk/pdbsum/8qvw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8qvw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SRP68_HUMAN SRP68_HUMAN] Signal-recognition-particle assembly has a crucial role in targeting secretory proteins to the rough endoplasmic reticulum membrane. SRP68 binds the 7S RNA, SRP72 binds to this complex subsequently. This ribonucleoprotein complex might interact directly with the docking protein in the ER membrane and possibly participate in the elongation arrest function.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The signal recognition particle (SRP) is a critical component in protein sorting pathways in all domains of life. Human SRP contains six proteins bound to the 7S RNA and their structures and functions have been mostly elucidated. The SRP68/72 dimer is the largest SRP component and is essential for SRP function. Although the structures of the SRP68/72 RNA binding and dimerization domains have been previously reported, the structure and function of large portions of the SRP68/72 dimer remain unknown. Here, we analyse full-length SRP68/72 using cryo-EM and report that SRP68/72 depend on each other for stability and form an extended dimerization domain. This newly observed dimerization domain is both a protein- and RNA-binding domain. Comparative analysis with current structural models suggests that this dimerization domain undergoes dramatic translocation upon SRP docking onto SRP receptor and eventually comes close to the Alu domain. We propose that the SRP68/72 dimerization domain functions by binding and detaching the Alu domain and SRP9/14 from the ribosomal surface, thus releasing elongation arrest upon docking onto the ER membrane.

Cryo-EM structure of SRP68/72 reveals an extended dimerization domain with RNA-binding activity.,Zhong Y, Feng J, Koh AF, Kotecha A, Greber BJ, Ataide SF Nucleic Acids Res. 2024 May 22;52(9):5285-5300. doi: 10.1093/nar/gkae107. PMID:38366771<ref>PMID:38366771</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8qvw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Ataide SF]]
[[Category: Feng J]]
[[Category: Greber BJ]]
[[Category: Koh AF]]
[[Category: Kotecha A]]
[[Category: Zhong Y]]