4bwe

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m (Protected "4bwe" [edit=sysop:move=sysop])
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'''Unreleased structure'''
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{{STRUCTURE_4bwe| PDB=4bwe | SCENE= }}
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===Crystal structure of C-terminally truncated glypican-1 after controlled dehydration to 86 percent relative humidity===
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{{ABSTRACT_PUBMED_24311593}}
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The entry 4bwe is ON HOLD
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==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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Authors: Awad, W., Svensson Birkedal, G., Thunnissen, M.M.G.M., Mani, K., Logan, D.T.
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==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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Description: Crystal structure of C-terminally truncated glypican-1 after controlled dehydration to 86 percent relative humidity
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==About this Structure==
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[[4bwe]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BWE OCA].
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==Reference==
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<ref group="xtra">PMID:024311593</ref><references group="xtra"/><references/>
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[[Category: Awad, W.]]
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[[Category: Birkedal, G Svensson.]]
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[[Category: Logan, D T.]]
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[[Category: Mani, K.]]
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[[Category: Thunnissen, M M.G M.]]
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[[Category: Glycoprotein]]
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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]]

Revision as of 10:19, 18 December 2013

Template:STRUCTURE 4bwe

Contents

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

Template:ABSTRACT PUBMED 24311593

Disease

[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

[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.[1] [2]

About this Structure

4bwe is a 4 chain structure. Full crystallographic information is available from OCA.

Reference

  • Awad W, Svensson Birkedal G, Thunnissen MM, Mani K, Logan DT. Improvements in the order, isotropy and electron density of glypican-1 crystals by controlled dehydration. Acta Crystallogr D Biol Crystallogr. 2013 Dec;69(Pt 12):2524-33. doi:, 10.1107/S0907444913025250. Epub 2013 Nov 19. PMID:24311593 doi:http://dx.doi.org/10.1107/S0907444913025250
  1. ↑ Taylor DR, Whitehouse IJ, Hooper NM. Glypican-1 mediates both prion protein lipid raft association and disease isoform formation. PLoS Pathog. 2009 Nov;5(11):e1000666. doi: 10.1371/journal.ppat.1000666. Epub, 2009 Nov 20. PMID:19936054 doi:10.1371/journal.ppat.1000666
  2. ↑ Cheng F, Cappai R, Ciccotosto GD, Svensson G, Multhaup G, Fransson LA, Mani K. Suppression of amyloid beta A11 antibody immunoreactivity by vitamin C: possible role of heparan sulfate oligosaccharides derived from glypican-1 by ascorbate-induced, nitric oxide (NO)-catalyzed degradation. J Biol Chem. 2011 Aug 5;286(31):27559-72. doi: 10.1074/jbc.M111.243345. Epub 2011, Jun 3. PMID:21642435 doi:http://dx.doi.org/10.1074/jbc.M111.243345

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