4gxb

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:51, 20 March 2024) (edit) (undo)
 
(One intermediate revision not shown.)
Line 1: Line 1:
==Structure of the SNX17 atypical FERM domain bound to the NPxY motif of P-selectin==
==Structure of the SNX17 atypical FERM domain bound to the NPxY motif of P-selectin==
-
<StructureSection load='4gxb' size='340' side='right' caption='[[4gxb]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
+
<StructureSection load='4gxb' size='340' side='right'caption='[[4gxb]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[4gxb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [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=4GXB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GXB FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[4gxb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GXB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4GXB FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
-
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3lui|3lui]], [[3fog|3fog]], [[1hes|1hes]]</td></tr>
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
-
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SNX17 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), Selp ([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'>[https://proteopedia.org/fgij/fg.htm?mol=4gxb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gxb OCA], [https://pdbe.org/4gxb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4gxb RCSB], [https://www.ebi.ac.uk/pdbsum/4gxb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4gxb ProSAT]</span></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=4gxb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gxb OCA], [http://pdbe.org/4gxb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4gxb RCSB], [http://www.ebi.ac.uk/pdbsum/4gxb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4gxb ProSAT]</span></td></tr>
+
</table>
</table>
== Function ==
== Function ==
-
[[http://www.uniprot.org/uniprot/SNX17_HUMAN SNX17_HUMAN]] Critical regulator of endosomal recycling of numerous receptors, channels, and other transmembrane proteins. Binds to NPxY sequences in the cytoplasmic tails of target cargos. Plays a role in the sorting of endocytosed LRP1 and APP, and prevents their degradation. Required for maintenance of normal cell surface levels of APP and LRP1. Recycles internalized integrins ITGB1, ITGB5 and their associated alpha subunits, preventing them from lysosomal degradation. Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)).<ref>PMID:15121882</ref> <ref>PMID:15769472</ref> <ref>PMID:16712798</ref> <ref>PMID:19005208</ref> <ref>PMID:22492727</ref> <ref>PMID:21512128</ref> [[http://www.uniprot.org/uniprot/LYAM3_MOUSE LYAM3_MOUSE]] Ca(2+)-dependent receptor for myeloid cells that binds to carbohydrates on neutrophils and monocytes. Mediates the interaction of activated endothelial cells or platelets with leukocytes. The ligand recognized is sialyl-Lewis X. Mediates rapid rolling of leukocyte rolling over vascular surfaces during the initial steps in inflammation through interaction with PSGL1.<ref>PMID:12370362</ref>
+
[https://www.uniprot.org/uniprot/SNX17_HUMAN SNX17_HUMAN] Critical regulator of endosomal recycling of numerous receptors, channels, and other transmembrane proteins. Binds to NPxY sequences in the cytoplasmic tails of target cargos. Plays a role in the sorting of endocytosed LRP1 and APP, and prevents their degradation. Required for maintenance of normal cell surface levels of APP and LRP1. Recycles internalized integrins ITGB1, ITGB5 and their associated alpha subunits, preventing them from lysosomal degradation. Interacts with membranes containing phosphatidylinositol 3-phosphate (PtdIns(3P)).<ref>PMID:15121882</ref> <ref>PMID:15769472</ref> <ref>PMID:16712798</ref> <ref>PMID:19005208</ref> <ref>PMID:22492727</ref> <ref>PMID:21512128</ref>
-
<div style="background-color:#fffaf0;">
+
-
== Publication Abstract from PubMed ==
+
-
Transit of proteins through the endosomal organelle following endocytosis is critical for regulating the homeostasis of cell-surface proteins and controlling signal transduction pathways. However, the mechanisms that control these membrane-transport processes are poorly understood. The Phox-homology (PX) domain-containing proteins sorting nexin (SNX) 17, SNX27, and SNX31 have emerged recently as key regulators of endosomal recycling and bind conserved Asn-Pro-Xaa-Tyr-sorting signals in transmembrane cargos via an atypical band, 4.1/ezrin/radixin/moesin (FERM) domain. Here we present the crystal structure of the SNX17 FERM domain bound to the sorting motif of the P-selectin adhesion protein, revealing both the architecture of the atypical FERM domain and the molecular basis for recognition of these essential sorting sequences. We further show that the PX-FERM proteins share a promiscuous ability to bind a wide array of putative cargo molecules, including receptor tyrosine kinases, and propose a model for their coordinated molecular interactions with membrane, cargo, and regulatory proteins.
+
-
 
+
-
Structural basis for endosomal trafficking of diverse transmembrane cargos by PX-FERM proteins.,Ghai R, Bugarcic A, Liu H, Norwood SJ, Skeldal S, Coulson EJ, Li SS, Teasdale RD, Collins BM Proc Natl Acad Sci U S A. 2013 Feb 19;110(8):E643-52. doi:, 10.1073/pnas.1216229110. Epub 2013 Feb 4. PMID:23382219<ref>PMID:23382219</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 4gxb" style="background-color:#fffaf0;"></div>
+
==See Also==
==See Also==
*[[Selectin|Selectin]]
*[[Selectin|Selectin]]
-
*[[Sorting nexin|Sorting nexin]]
+
*[[Sorting nexin 3D structures|Sorting nexin 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Human]]
+
[[Category: Homo sapiens]]
-
[[Category: Lk3 transgenic mice]]
+
[[Category: Large Structures]]
-
[[Category: Bugarcic, A]]
+
[[Category: Mus musculus]]
-
[[Category: Collins, B M]]
+
[[Category: Bugarcic A]]
-
[[Category: Ghai, R]]
+
[[Category: Collins BM]]
-
[[Category: Li, S S]]
+
[[Category: Ghai R]]
-
[[Category: Liu, H]]
+
[[Category: Li SS]]
-
[[Category: Norwood, S J]]
+
[[Category: Liu H]]
-
[[Category: Teasdale, R D]]
+
[[Category: Norwood SJ]]
-
[[Category: Ferm domain]]
+
[[Category: Teasdale RD]]
-
[[Category: Protein transport-cell adhesion complex]]
+

Current revision

Structure of the SNX17 atypical FERM domain bound to the NPxY motif of P-selectin

PDB ID 4gxb

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4gxb"
Personal tools