4ymr: Difference between revisions

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-'''Unreleased structure'''
+==Crystal structure of the domain swapped PXB/TPR domain of mouse SNX21==
+<StructureSection load='4ymr' size='340' side='right' caption='[[4ymr]], [[Resolution|resolution]] 2.40&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4ymr]] is a 2 chain structure. 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='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://www.rcsb.org/pdb/explore.do?structureId=4ymr RCSB], [http://www.ebi.ac.uk/pdbsum/4ymr PDBsum]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== 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.
-The entry 4ymr is ON HOLD  until Paper Publication
+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<ref>PMID:25882846</ref>
-Authors: Collins, B.C., Teasdale, R.D., Clairfeuille, T.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description: Crystal structure of the domain swapped PXB/TPR domain of mouse SNX21
+== References ==
-[[Category: Unreleased Structures]]
+<references/>
-[[Category: Collins, B.C]]
+__TOC__
+</StructureSection>
 [[Category: Clairfeuille, T]]
-[[Category: Teasdale, R.D]]
+[[Category: Collins, B C]]
+[[Category: Teasdale, R D]]
+[[Category: Tetratricopeptide repeat endosome trafficking]]