1n99: Difference between revisions
New page: left|200px<br /> <applet load="1n99" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n99, resolution 1.94Å" /> '''CRYSTAL STRUCTURE O... |
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== | ==CRYSTAL STRUCTURE OF THE PDZ TANDEM OF HUMAN SYNTENIN== | ||
Syntenin, a 33 kDa protein, interacts with several cell membrane receptors | <StructureSection load='1n99' size='340' side='right'caption='[[1n99]], [[Resolution|resolution]] 1.94Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1n99]] 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=1N99 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N99 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.94Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=1n99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n99 OCA], [https://pdbe.org/1n99 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n99 RCSB], [https://www.ebi.ac.uk/pdbsum/1n99 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n99 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SDCB1_HUMAN SDCB1_HUMAN] Seems to function as an adapter protein. In adherens junctions may function to couple syndecans to cytoskeletal proteins or signaling components. Seems to couple transcription factor SOX4 to the IL-5 receptor (IL5RA). May also play a role in vesicular trafficking. Seems to be required for the targeting of TGFA to the cell surface in the early secretory pathway.<ref>PMID:10230395</ref> <ref>PMID:11179419</ref> <ref>PMID:11498591</ref> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/n9/1n99_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1n99 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Syntenin, a 33 kDa protein, interacts with several cell membrane receptors and with merlin, the product of the causal gene for neurofibromatosis type II. We report a crystal structure of the functional fragment of human syntenin containing two canonical PDZ domains, as well as binding studies for full-length syntenin, the PDZ tandem, and isolated PDZ domains. We show that the functional properties of syntenin are a result of independent interactions with target peptides, and that each domain is able to bind peptides belonging to two different classes: PDZ1 binds peptides from classes I and III, while PDZ2 interacts with classes I and II. The independent binding of merlin by PDZ1 and syndecan-4 by PDZ2 provides direct evidence for the coupling of syndecan-mediated signaling to actin regulation by merlin. | |||
PDZ tandem of human syntenin: crystal structure and functional properties.,Kang BS, Cooper DR, Jelen F, Devedjiev Y, Derewenda U, Dauter Z, Otlewski J, Derewenda ZS Structure. 2003 Apr;11(4):459-68. PMID:12679023<ref>PMID:12679023</ref> | |||
== | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | |||
<div class="pdbe-citations 1n99" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[3D structures of syntenin|3D structures of syntenin]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Cooper | [[Category: Cooper DR]] | ||
[[Category: Dauter | [[Category: Dauter Z]] | ||
[[Category: Derewenda | [[Category: Derewenda U]] | ||
[[Category: Derewenda | [[Category: Derewenda ZS]] | ||
[[Category: Devedjiev | [[Category: Devedjiev Y]] | ||
[[Category: Jelen | [[Category: Jelen F]] | ||
[[Category: Kang | [[Category: Kang BS]] | ||
[[Category: Otlewski | [[Category: Otlewski J]] | ||
