4ymr: Difference between revisions

<StructureSection load='4ymr' size='340' side='right' caption='[[4ymr]], [[Resolution|resolution]] 2.40&Aring;' scene=''>

<table><tr><td colspan='2'>[[4ymr]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4YMR FirstGlance]. <br>

</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Snx21 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ymr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ymr OCA], [http://pdbe.org/4ymr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4ymr RCSB], [http://www.ebi.ac.uk/pdbsum/4ymr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4ymr ProSAT]</span></td></tr>

== Publication Abstract from PubMed ==

Sorting 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.

 

<div class="pdbe-citations 4ymr" style="background-color:#fffaf0;"></div>

[[Category: Lk3 transgenic mice]]

[[Category: Clairfeuille, T]]

[[Category: Collins, B C]]

[[Category: Teasdale, R D]]

[[Category: Protein transport]]

[[Category: Tetratricopeptide repeat endosome trafficking]]