4bwe

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==Crystal structure of C-terminally truncated glypican-1 after controlled dehydration to 86 percent relative humidity==
==Crystal structure of C-terminally truncated glypican-1 after controlled dehydration to 86 percent relative humidity==
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<StructureSection load='4bwe' size='340' side='right' caption='[[4bwe]], [[Resolution|resolution]] 2.46&Aring;' scene=''>
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<StructureSection load='4bwe' size='340' side='right'caption='[[4bwe]], [[Resolution|resolution]] 2.46&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4bwe]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BWE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BWE FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4bwe]] is a 4 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=4BWE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BWE FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GPC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4bwe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bwe OCA], [https://pdbe.org/4bwe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4bwe RCSB], [https://www.ebi.ac.uk/pdbsum/4bwe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4bwe ProSAT]</span></td></tr>
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<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=4bwe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4bwe OCA], [http://pdbe.org/4bwe PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4bwe RCSB], [http://www.ebi.ac.uk/pdbsum/4bwe PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4bwe ProSAT]</span></td></tr>
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</table>
</table>
== Disease ==
== Disease ==
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[[http://www.uniprot.org/uniprot/GPC1_HUMAN GPC1_HUMAN]] Biliary atresia. Associates (via the heparan sulfate side chains) with fibrillar APP-beta amyloid peptides in primitive and classic amyloid plaques and may be involved in the deposition of these senile plaques in the Alzheimer disease (AD) brain. Misprocessing of GPC1 is found in fibroblasts of patients with Niemann-Pick Type C1 disease. This is due to the defective deaminative degradation of heparan sulfate chains.
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[[https://www.uniprot.org/uniprot/GPC1_HUMAN GPC1_HUMAN]] Biliary atresia. Associates (via the heparan sulfate side chains) with fibrillar APP-beta amyloid peptides in primitive and classic amyloid plaques and may be involved in the deposition of these senile plaques in the Alzheimer disease (AD) brain. Misprocessing of GPC1 is found in fibroblasts of patients with Niemann-Pick Type C1 disease. This is due to the defective deaminative degradation of heparan sulfate chains.
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/GPC1_HUMAN GPC1_HUMAN]] Cell surface proteoglycan that bears heparan sulfate. Binds, via the heparan sulfate side chains, alpha-4 (V) collagen and participates in Schwann cell myelination (By similarity). May act as a catalyst in increasing the rate of conversion of prion protein PRPN(C) to PRNP(Sc) via associating (via the heparan sulfate side chains) with both forms of PRPN, targeting them to lipid rafts and facilitating their interaction. Required for proper skeletal muscle differentiation by sequestering FGF2 in lipid rafts preventing its binding to receptors (FGFRs) and inhibiting the FGF-mediated signaling.<ref>PMID:19936054</ref> <ref>PMID:21642435</ref>
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[[https://www.uniprot.org/uniprot/GPC1_HUMAN GPC1_HUMAN]] Cell surface proteoglycan that bears heparan sulfate. Binds, via the heparan sulfate side chains, alpha-4 (V) collagen and participates in Schwann cell myelination (By similarity). May act as a catalyst in increasing the rate of conversion of prion protein PRPN(C) to PRNP(Sc) via associating (via the heparan sulfate side chains) with both forms of PRPN, targeting them to lipid rafts and facilitating their interaction. Required for proper skeletal muscle differentiation by sequestering FGF2 in lipid rafts preventing its binding to receptors (FGFRs) and inhibiting the FGF-mediated signaling.<ref>PMID:19936054</ref> <ref>PMID:21642435</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The use of controlled dehydration for improvement of protein crystal diffraction quality is increasing in popularity, although there are still relatively few documented examples of success. A study has been carried out to establish whether controlled dehydration could be used to improve the anisotropy of crystals of the core protein of the human proteoglycan glypican-1. Crystals were subjected to controlled dehydration using the HC1 device. The optimal protocol for dehydration was developed by careful investigation of the following parameters: dehydration rate, final relative humidity and total incubation time Tinc. Of these, the most important was shown to be Tinc. After dehydration using the optimal protocol the crystals showed significantly reduced anisotropy and improved electron density, allowing the building of previously disordered parts of the structure.
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Improvements in the order, isotropy and electron density of glypican-1 crystals by controlled dehydration.,Awad W, Svensson Birkedal G, Thunnissen MM, Mani K, Logan DT Acta Crystallogr D Biol Crystallogr. 2013 Dec;69(Pt 12):2524-33. doi:, 10.1107/S0907444913025250. Epub 2013 Nov 19. PMID:24311593<ref>PMID:24311593</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4bwe" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Human]]
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[[Category: Homo sapiens]]
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[[Category: Awad, W]]
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[[Category: Large Structures]]
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[[Category: Birkedal, G Svensson]]
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[[Category: Awad W]]
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[[Category: Logan, D T]]
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[[Category: Logan DT]]
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[[Category: Mani, K]]
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[[Category: Mani K]]
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[[Category: Thunnissen, M M.G M]]
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[[Category: Svensson Birkedal G]]
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[[Category: Glycoprotein]]
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[[Category: Thunnissen MMGM]]
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[[Category: Glycosaminoglycan]]
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[[Category: Helical bundle]]
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[[Category: Heparan sulfate]]
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[[Category: Membrane protein]]
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[[Category: Proteoglycan]]
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Revision as of 17:12, 7 September 2022

Crystal structure of C-terminally truncated glypican-1 after controlled dehydration to 86 percent relative humidity

PDB ID 4bwe

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