4ymr: Difference between revisions
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==Crystal structure of the domain swapped PXB/TPR domain of mouse SNX21== | ==Crystal structure of the domain swapped PXB/TPR domain of mouse SNX21== | ||
<StructureSection load='4ymr' size='340' side='right' caption='[[4ymr]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='4ymr' size='340' side='right'caption='[[4ymr]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ymr]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4ymr]] 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=4YMR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4YMR FirstGlance]. <br> | ||
</td></tr> | </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=4ymr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ymr OCA], [https://pdbe.org/4ymr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ymr RCSB], [https://www.ebi.ac.uk/pdbsum/4ymr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ymr ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/SNX21_MOUSE SNX21_MOUSE] Binds to membranes enriched in phosphatidylinositol 3-phosphate (PtdIns(P3)) and phosphatidylinositol 4,5-bisphosphate (PubMed:25882846). May be involved in several stages of intracellular trafficking.<ref>PMID:25882846</ref> | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 4ymr" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 4ymr" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Sorting nexin 3D structures|Sorting nexin 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Mus musculus]] | ||
[[Category: | [[Category: Clairfeuille T]] | ||
[[Category: | [[Category: Collins BC]] | ||
[[Category: | [[Category: Teasdale RD]] | ||
Revision as of 11:19, 3 May 2023
Crystal structure of the domain swapped PXB/TPR domain of mouse SNX21Crystal structure of the domain swapped PXB/TPR domain of mouse SNX21
Structural highlights
FunctionSNX21_MOUSE Binds to membranes enriched in phosphatidylinositol 3-phosphate (PtdIns(P3)) and phosphatidylinositol 4,5-bisphosphate (PubMed:25882846). May be involved in several stages of intracellular trafficking.[1] Publication Abstract from PubMedSorting nexins (SNX) orchestrate membrane trafficking and signalling events required for the proper distribution of proteins within the endosomal network. Their phox homology (PX) domain acts as a phosphinositide (PI) recognition module that targets them to specific endocytic membrane domains. The modularity of SNX proteins confers a wide variety of functions from signalling to membrane deformation and cargo binding, and many SNXs are crucial modulators of endosome dynamics and are involved in a myriad of physiological and pathological processes such as neurodegenerative diseases, cancer and inflammation. Here, we have studied the poorly characterized SNX20 and its paralogue SNX21, which contain an N-terminal PX domain and a C-terminal PX-associated B (PXB) domain of unknown function. The two proteins share similar PI-binding properties and are recruited to early endosomal compartments by their PX domain. The crystal structure of the SNX21 PXB domain reveals a tetratricopeptide repeat (TPR) fold, a module that typically binds short peptide motifs, with three TPR alpha-helical repeats. However, the C-terminal capping helix adopts a highly unusual and potentially self-inhibitory topology. SAXS solution structures of SNX20 and SNX21 show that these proteins adopt a compact globular architecture, and membrane interaction analyses indicate the presence of overlapping PI-binding sites that may regulate their intracellular localisation. This study provides the first structural analysis of this poorly characterized subfamily of SNX proteins, highlighting a likely role as endosome-associated scaffolds. Structure and membrane binding properties of the endosomal tetratricopeptide repeat (TPR) domain-containing sorting nexins SNX20 and SNX21.,Clairfeuille T, Norwood SJ, Qi X, Teasdale RD, Collins BM J Biol Chem. 2015 Apr 16. pii: jbc.M115.650598. PMID:25882846[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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