View source for 5woe


==Solution structure of the sorting nexin 25 phox-homology domain==
<StructureSection load='5woe' size='340' side='right'caption='[[5woe]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5woe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WOE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WOE FirstGlance]. <br>
</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=5woe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5woe OCA], [https://pdbe.org/5woe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5woe RCSB], [https://www.ebi.ac.uk/pdbsum/5woe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5woe ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SNX25_HUMAN SNX25_HUMAN] May be involved in several stages of intracellular trafficking.
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== Publication Abstract from PubMed ==
Phox homology (PX) domains are membrane interacting domains that bind to phosphatidylinositol phospholipids or phosphoinositides, markers of organelle identity in the endocytic system. Although many PX domains bind the canonical endosome-enriched lipid PtdIns3P, others interact with alternative phosphoinositides, and a precise understanding of how these specificities arise has remained elusive. Here we systematically screen all human PX domains for their phospholipid preferences using liposome binding assays, biolayer interferometry and isothermal titration calorimetry. These analyses define four distinct classes of human PX domains that either bind specifically to PtdIns3P, non-specifically to various di- and tri-phosphorylated phosphoinositides, bind both PtdIns3P and other phosphoinositides, or associate with none of the lipids tested. A comprehensive evaluation of PX domain structures reveals two distinct binding sites that explain these specificities, providing a basis for defining and predicting the functional membrane interactions of the entire PX domain protein family.

Classification of the human phox homology (PX) domains based on their phosphoinositide binding specificities.,Chandra M, Chin YK, Mas C, Feathers JR, Paul B, Datta S, Chen KE, Jia X, Yang Z, Norwood SJ, Mohanty B, Bugarcic A, Teasdale RD, Henne WM, Mobli M, Collins BM Nat Commun. 2019 Apr 4;10(1):1528. doi: 10.1038/s41467-019-09355-y. PMID:30948714<ref>PMID:30948714</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5woe" style="background-color:#fffaf0;"></div>

==See Also==
*[[Sorting nexin 3D structures|Sorting nexin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Chin YKY]]
[[Category: Collins BM]]
[[Category: Mas C]]
[[Category: Mobli M]]