View source for 7wf9


==Crystal structure of mouse SNX25 RGS domain in space group P41212==
<StructureSection load='7wf9' size='340' side='right'caption='[[7wf9]], [[Resolution|resolution]] 2.55&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7wf9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7WF9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WF9 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]] 2.55&#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=7wf9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wf9 OCA], [https://pdbe.org/7wf9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wf9 RCSB], [https://www.ebi.ac.uk/pdbsum/7wf9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wf9 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SNX25_MOUSE SNX25_MOUSE] May be involved in several stages of intracellular trafficking.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
As a subgroup of sorting nexins (SNXs) that contain regulator of G protein signaling homology (RH) domain, SNX-RH proteins, including SNX13, SNX14 and SNX25, were proposed to play bifunctional roles in protein sorting and GPCR signaling regulation. However, mechanistic details of SNX-RH proteins functioning via RH domain remain to be illustrated. Here, we delineate crystal structures of the RH domains of SNX13 and SNX25, revealing a homodimer of SNX13 RH domain mediated by unique extended alpha4 and alpha5 helices, and a thiol modulated homodimer of SNX25-RH triggered by a unique cysteine on alpha6 helix. Further studies showed that RH domains of SNX-RH do not possess binding capacity toward Galpha subunits, owing to the lack of critical residues for interaction. Thus, this study identifies a group of novel non-canonical RH domains that can act as a dimerization module in sorting nexins, which provides structural basis for mechanism studies on SNX-RH protein functions.

Structural Studies Reveal Unique Non-canonical Regulators of G Protein Signaling Homology (RH) Domains in Sorting Nexins.,Zhang Y, Chen R, Dong Y, Zhu J, Su K, Liu J, Xu J J Mol Biol. 2022 Nov 15;434(21):167823. doi: 10.1016/j.jmb.2022.167823. Epub 2022 , Sep 11. PMID:36103920<ref>PMID:36103920</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7wf9" style="background-color:#fffaf0;"></div>

==See Also==
*[[Sorting nexin 3D structures|Sorting nexin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Liu J]]
[[Category: Xu J]]
[[Category: Zhang Y]]