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1. (CSDB ID: 7363) | report error |
| a-D-Manp-(1-2)-+ /Variants 0/-+ /Variants 1/-+ | | | Subst-(1-2)-EtN-(1--P--6)--a-D-Manp-(1-2)-a-D-Manp-(1-6)-a-D-Manp-(1-4)-a-D-GlcpN-(1-6)-myoIno-(1--P--3)--Gro | /Variants 2/-+ /Variants 0/ is: 90%Pam-(1-2)- OR (exclusively) 10%Myr-(1-2)- /Variants 1/ is: 88%Ste-(1-2)- OR (exclusively) 12%Ole-(1-2)- /Variants 2/ is: 80%Ste-(1-1)- OR (exclusively) 4%Myr-(1-1)- OR (exclusively) 2%Beh-(1-1)- OR (exclusively) 2%Ach-(1-1)- OR (exclusively) 12%Pam-(1-1)- Subst = protein CSP, MSP-1 to MSP-10 | Show graphically |
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Plasmodium
(NCBI TaxID 5820,
species name lookup)
mpikg.mpg.deGlypiation is a common posttranslational modification of eukaryotic proteins involving the attachment of a glycosylphosphatidylinositol (GPI) glycolipid. GPIs contain a conserved phosphoglycan that is modified in a cell- and tissue-specific manner. GPI complexity suggests roles in biological processes and effects on the attached protein, but the difficulties to get homogeneous material have hindered studies. We disclose a one-pot intein-mediated ligation (OPL) to obtain GPI-anchored proteins. The strategy enables the glypiation of folded and denatured proteins with a natural linkage to the glycolipid. Using the strategy, glypiated eGFP, Thy1, and the Plasmodium berghei protein MSP1(19) were prepared. Glypiation did not alter the structure of eGFP and MSP1(19) proteins in solution, but it induced a strong pro-inflammatory response in vitro. The strategy provides access to glypiated proteins to elucidate the activity of this modification and for use as vaccine candidates against parasitic infections.
glycolipid, Plasmodium, GPI anchor, glypiation, protein modifications, protein semisynthesis
Structure type: oligomerlXSte(1-1)[lXPam(1-2)[aDManp(1-2)[Subst(1-2)xXEtN(1-P-6)]aDManp(1-2)aDManp(1-6)aDManp(1-4)aDGlcpN(1-6)]xXmyoIno(1-P-3),lXSte(1-2)]x?Gro // Subst = protein CSP, MSP-1 to MSP-10There is only one chemically distinct structure for the variant above:
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2. (CSDB ID: 8363) | report error |
| a-D-Manp-(1-2)-+ Ste-(1-1)-+ | | Cys-(1-2)-EtN-(1--P--6)--a-D-Manp-(1-2)-a-D-Manp-(1-6)-a-D-Manp-(1-4)-a-D-GlcpN-(1-6)-myoIno-(1--P--3)--Gro | Ste-(1-2)-+ | Show graphically |
|
Show legend Show as text |
Plasmodium
(NCBI TaxID 5820,
species name lookup)
mpikg.mpg.deGlypiation is a common posttranslational modification of eukaryotic proteins involving the attachment of a glycosylphosphatidylinositol (GPI) glycolipid. GPIs contain a conserved phosphoglycan that is modified in a cell- and tissue-specific manner. GPI complexity suggests roles in biological processes and effects on the attached protein, but the difficulties to get homogeneous material have hindered studies. We disclose a one-pot intein-mediated ligation (OPL) to obtain GPI-anchored proteins. The strategy enables the glypiation of folded and denatured proteins with a natural linkage to the glycolipid. Using the strategy, glypiated eGFP, Thy1, and the Plasmodium berghei protein MSP1(19) were prepared. Glypiation did not alter the structure of eGFP and MSP1(19) proteins in solution, but it induced a strong pro-inflammatory response in vitro. The strategy provides access to glypiated proteins to elucidate the activity of this modification and for use as vaccine candidates against parasitic infections.
glycolipid, Plasmodium, GPI anchor, glypiation, protein modifications, protein semisynthesis
Structure type: oligomer| New query | Export IDs | Home | Help |
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