4akv: Difference between revisions

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<StructureSection load='4akv' size='340' side='right'caption='[[4akv]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
<StructureSection load='4akv' size='340' side='right'caption='[[4akv]], [[Resolution|resolution]] 2.65&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4akv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AKV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AKV FirstGlance]. <br>
<table><tr><td colspan='2'>[[4akv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AKV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AKV FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.651&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4akv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4akv OCA], [https://pdbe.org/4akv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4akv RCSB], [https://www.ebi.ac.uk/pdbsum/4akv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4akv ProSAT]</span></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=4akv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4akv OCA], [https://pdbe.org/4akv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4akv RCSB], [https://www.ebi.ac.uk/pdbsum/4akv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4akv ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/SNX33_HUMAN SNX33_HUMAN]] Plays a role in the reorganization of the cytoskeleton, endocytosis and cellular vesicle trafficking via its interactions with membranes, WASL, DNM1 and DNM2. Acts both during interphase and at the end of mitotic cell divisions. Required for efficient progress through mitosis and cytokinesis. Required for normal formation of the cleavage furrow at the end of mitosis. Modulates endocytosis of cell-surface proteins, such as APP and PRNP; this then modulates the secretion of APP and PRNP peptides. Promotes membrane tubulation (in vitro). May promote the formation of macropinosomes.<ref>PMID:18353773</ref> <ref>PMID:18419754</ref> <ref>PMID:19487689</ref> <ref>PMID:20964629</ref> <ref>PMID:21048941</ref> <ref>PMID:22718350</ref>
[https://www.uniprot.org/uniprot/SNX33_HUMAN SNX33_HUMAN] Plays a role in the reorganization of the cytoskeleton, endocytosis and cellular vesicle trafficking via its interactions with membranes, WASL, DNM1 and DNM2. Acts both during interphase and at the end of mitotic cell divisions. Required for efficient progress through mitosis and cytokinesis. Required for normal formation of the cleavage furrow at the end of mitosis. Modulates endocytosis of cell-surface proteins, such as APP and PRNP; this then modulates the secretion of APP and PRNP peptides. Promotes membrane tubulation (in vitro). May promote the formation of macropinosomes.<ref>PMID:18353773</ref> <ref>PMID:18419754</ref> <ref>PMID:19487689</ref> <ref>PMID:20964629</ref> <ref>PMID:21048941</ref> <ref>PMID:22718350</ref>  


==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Arrowsmith, C]]
[[Category: Arrowsmith C]]
[[Category: Bountra, C]]
[[Category: Bountra C]]
[[Category: Delft, F von]]
[[Category: Edwards A]]
[[Category: Edwards, A]]
[[Category: Filippakopoulos P]]
[[Category: Filippakopoulos, P]]
[[Category: Froese DS]]
[[Category: Froese, D S]]
[[Category: Krojer T]]
[[Category: Krojer, T]]
[[Category: Muniz JRC]]
[[Category: Muniz, J R.C]]
[[Category: Oberholzer A]]
[[Category: Oberholzer, A]]
[[Category: Shrestha L]]
[[Category: Shrestha, L]]
[[Category: Weigelt J]]
[[Category: Weigelt, J]]
[[Category: Yue WW]]
[[Category: Yue, W W]]
[[Category: Von Delft F]]
[[Category: Organelle biogenesis]]
[[Category: Transport protein]]

Latest revision as of 13:51, 9 May 2024

Crystal structure of human sorting nexin 33 (SNX33)Crystal structure of human sorting nexin 33 (SNX33)

Structural highlights

4akv is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.651Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SNX33_HUMAN Plays a role in the reorganization of the cytoskeleton, endocytosis and cellular vesicle trafficking via its interactions with membranes, WASL, DNM1 and DNM2. Acts both during interphase and at the end of mitotic cell divisions. Required for efficient progress through mitosis and cytokinesis. Required for normal formation of the cleavage furrow at the end of mitosis. Modulates endocytosis of cell-surface proteins, such as APP and PRNP; this then modulates the secretion of APP and PRNP peptides. Promotes membrane tubulation (in vitro). May promote the formation of macropinosomes.[1] [2] [3] [4] [5] [6]

See Also

References

  1. ↑ Schobel S, Neumann S, Hertweck M, Dislich B, Kuhn PH, Kremmer E, Seed B, Baumeister R, Haass C, Lichtenthaler SF. A novel sorting nexin modulates endocytic trafficking and alpha-secretase cleavage of the amyloid precursor protein. J Biol Chem. 2008 May 23;283(21):14257-68. doi: 10.1074/jbc.M801531200. Epub 2008, Mar 19. PMID:18353773 doi:http://dx.doi.org/10.1074/jbc.M801531200
  2. ↑ Heiseke A, Schobel S, Lichtenthaler SF, Vorberg I, Groschup MH, Kretzschmar H, Schatzl HM, Nunziante M. The novel sorting nexin SNX33 interferes with cellular PrP formation by modulation of PrP shedding. Traffic. 2008 Jul;9(7):1116-29. doi: 10.1111/j.1600-0854.2008.00750.x. Epub 2008 , Apr 18. PMID:18419754 doi:http://dx.doi.org/10.1111/j.1600-0854.2008.00750.x
  3. ↑ Zhang J, Zhang X, Guo Y, Xu L, Pei D. Sorting nexin 33 induces mammalian cell micronucleated phenotype and actin polymerization by interacting with Wiskott-Aldrich syndrome protein. J Biol Chem. 2009 Aug 7;284(32):21659-69. doi: 10.1074/jbc.M109.007278. Epub 2009, Jun 1. PMID:19487689 doi:http://dx.doi.org/10.1074/jbc.M109.007278
  4. ↑ Dislich B, Than ME, Lichtenthaler SF. Specific amino acids in the BAR domain allow homodimerization and prevent heterodimerization of sorting nexin 33. Biochem J. 2011 Jan 1;433(1):75-83. doi: 10.1042/BJ20100709. PMID:20964629 doi:http://dx.doi.org/10.1042/BJ20100709
  5. ↑ Wang JT, Kerr MC, Karunaratne S, Jeanes A, Yap AS, Teasdale RD. The SNX-PX-BAR family in macropinocytosis: the regulation of macropinosome formation by SNX-PX-BAR proteins. PLoS One. 2010 Oct 29;5(10):e13763. doi: 10.1371/journal.pone.0013763. PMID:21048941 doi:10.1371/journal.pone.0013763
  6. ↑ Ma MP, Chircop M. SNX9, SNX18 and SNX33 are required for progression through and completion of mitosis. J Cell Sci. 2012 Sep 15;125(Pt 18):4372-82. doi: 10.1242/jcs.105981. Epub 2012, Jun 20. PMID:22718350 doi:http://dx.doi.org/10.1242/jcs.105981

4akv, resolution 2.65Å

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