View source for 3lh8


==Crystal structure of mouse VPS26B in spacegroup P41 21 2==
<StructureSection load='3lh8' size='340' side='right'caption='[[3lh8]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3lh8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3LH8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3LH8 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]] 2.6&#8491;</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=3lh8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3lh8 OCA], [https://pdbe.org/3lh8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3lh8 RCSB], [https://www.ebi.ac.uk/pdbsum/3lh8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3lh8 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/VP26B_MOUSE VP26B_MOUSE] Probable component of the retromer complex, a complex required to retrieve lysosomal enzyme receptors (IGF2R and M6PR) from endosomes to the trans-Golgi network.
== 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/lh/3lh8_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=3lh8 ConSurf].
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== Publication Abstract from PubMed ==
Retromer is a peripheral membrane protein complex that has pleiotropic roles in endosomal membrane trafficking. The core of retromer possesses three subunits VPS35, VPS29 and VPS26 that play different roles in binding to cargo, regulatory proteins and complex stabilisation. We have performed an investigation of the thermodynamics of core retromer assembly using isothermal titration calorimetry (ITC) demonstrating that VPS35 acts as the central subunit to which VPS29 and VPS26 bind independently. Furthermore we confirm that the conserved PRLYL motif of the large VPS35 subunit is critical for direct VPS26 interaction. Heat capacity measurements of VPS29 and VPS26 binding to VPS35 indicate extensive binding interfaces and suggest conformational alterations in VPS29 or VPS35 upon complex formation. Solution studies of the retromer core using small angle X-ray scattering, allow us to propose a model whereby VPS35 forms an extended platform with VPS29 and VPS26 bound at distal ends, with the potential for forming dimeric assemblies.

Assembly and solution structure of the core retromer protein complex.,Norwood SJ, Shaw DJ, Cowieson NP, Owen DJ, Teasdale RD, Collins BM Traffic. 2010 Sep 28. doi: 10.1111/j.1600-0854.2010.01124.x. PMID:20875039<ref>PMID:20875039</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3lh8" style="background-color:#fffaf0;"></div>

==See Also==
*[[Vacuolar protein sorting-associated protein 3D structures|Vacuolar protein sorting-associated protein 3D structures]]
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Collins B]]
[[Category: Norwood S]]
[[Category: Shaw D]]