2x43: Difference between revisions
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==STRUCTURAL BASIS OF MOLECULAR RECOGNITION BY SHERP AT MEMBRANE SURFACES== | |||
<StructureSection load='2x43' size='340' side='right'caption='[[2x43]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2x43]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X43 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X43 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=2x43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x43 OCA], [https://pdbe.org/2x43 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x43 RCSB], [https://www.ebi.ac.uk/pdbsum/2x43 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x43 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The 57-residue small hydrophilic endoplasmic reticulum-associated protein (SHERP) shows highly specific, stage-regulated expression in the non-replicative vector-transmitted stages of the kinetoplastid parasite, Leishmania major, the causative agent of human cutaneous leishmaniasis. Previous studies have demonstrated that SHERP localises as a peripheral membrane protein on the cytosolic face of the endoplasmic reticulum and on outer mitochondrial membranes while its high copy number suggests a critical function in vivo. However, the absence of defined domains or identifiable orthologues, together with lack of a clear phenotype in transgenic parasites lacking SHERP, has limited functional understanding of this protein. Here, we use a combination of biophysical and biochemical methods to demonstrate that SHERP can be induced to adopt a globular fold in the presence of anionic lipids or sodium dodecyl sulfate. Crosslinking and binding studies suggest that SHERP has the potential to form a complex with the vacuolar type H+-ATPase. Taken together, these results suggest that SHERP may function in modulating cellular processes related to membrane organization and/or acidification during vector transmission of infective Leishmania. | |||
Structural basis of molecular recognition the Leishmania small hydrophillic endoplasmic reticulum-associated protein, SHERP, at membrane surfaces.,Moore B, Miles AJ, Guerra-Giraldez C, Simpson PJ, Iwata M, Wallace BA, Matthews SJ, Smith DF, Brown KA J Biol Chem. 2010 Nov 24. PMID:21106528<ref>PMID:21106528</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2x43" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Brown, K A]] | |||
[[Category: Guerra, C G]] | |||
[[Category: Iwata, M]] | |||
[[Category: Matthews, S J]] | |||
[[Category: Miles, A J]] | |||
[[Category: Moore, B]] | |||
[[Category: Simpson, P]] | |||
[[Category: Smith, D F]] | |||
[[Category: Wallace, B A]] | |||
[[Category: Membrane protein]] | |||
Latest revision as of 05:24, 10 August 2022
STRUCTURAL BASIS OF MOLECULAR RECOGNITION BY SHERP AT MEMBRANE SURFACES
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