8i26: Difference between revisions
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The entry | ==NMR structure of Toxoplasma gondii PDCD5 (cis form)== | ||
<StructureSection load='8i26' size='340' side='right'caption='[[8i26]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8i26]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Toxoplasma_gondii_GT1 Toxoplasma gondii GT1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8I26 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8I26 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=8i26 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8i26 OCA], [https://pdbe.org/8i26 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8i26 RCSB], [https://www.ebi.ac.uk/pdbsum/8i26 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8i26 ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Toxoplasmosis, caused by Toxoplasma gondii, poses risks to vulnerable populations. TgPDCD5, a secreted protein of T. gondii, induces apoptosis through heparan sulfate-mediated endocytosis. The entry mechanism of TgPDCD5 has remained elusive. Here, we present the solution structure of TgPDCD5 as a helical bundle with an extended N-terminal helix, exhibiting molten globule characteristics. NMR perturbation studies reveal heparin/heparan sulfate binding involving the heparan sulfate/heparin proteoglycans-binding motif and the core region, influenced by proline isomerization of P107 residue. The heterogeneous proline recruits a cyclophilin TgCyp18, accelerating interconversion between conformers and regulating heparan/heparin binding. These atomic-level insights elucidate the binary switch's functionality, expose novel heparan sulfate-binding surfaces, and illuminate the unconventional cellular entry of pathogenic TgPDCD5. | |||
Proline Isomerization and Molten Globular Property of TgPDCD5 Secreted from Toxoplasma gondii Confers Its Regulation of Heparin Sulfate Binding.,Lin GM, Yu TA, Chang CF, Hsu CH JACS Au. 2024 Mar 20;4(5):1763-1774. doi: 10.1021/jacsau.3c00577. eCollection , 2024 May 27. PMID:38818051<ref>PMID:38818051</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Hsu | <div class="pdbe-citations 8i26" style="background-color:#fffaf0;"></div> | ||
[[Category: Lin | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Toxoplasma gondii GT1]] | |||
[[Category: Hsu CH]] | |||
[[Category: Lin MH]] | |||
Latest revision as of 08:25, 12 June 2024
NMR structure of Toxoplasma gondii PDCD5 (cis form)NMR structure of Toxoplasma gondii PDCD5 (cis form)
Structural highlights
Publication Abstract from PubMedToxoplasmosis, caused by Toxoplasma gondii, poses risks to vulnerable populations. TgPDCD5, a secreted protein of T. gondii, induces apoptosis through heparan sulfate-mediated endocytosis. The entry mechanism of TgPDCD5 has remained elusive. Here, we present the solution structure of TgPDCD5 as a helical bundle with an extended N-terminal helix, exhibiting molten globule characteristics. NMR perturbation studies reveal heparin/heparan sulfate binding involving the heparan sulfate/heparin proteoglycans-binding motif and the core region, influenced by proline isomerization of P107 residue. The heterogeneous proline recruits a cyclophilin TgCyp18, accelerating interconversion between conformers and regulating heparan/heparin binding. These atomic-level insights elucidate the binary switch's functionality, expose novel heparan sulfate-binding surfaces, and illuminate the unconventional cellular entry of pathogenic TgPDCD5. Proline Isomerization and Molten Globular Property of TgPDCD5 Secreted from Toxoplasma gondii Confers Its Regulation of Heparin Sulfate Binding.,Lin GM, Yu TA, Chang CF, Hsu CH JACS Au. 2024 Mar 20;4(5):1763-1774. doi: 10.1021/jacsau.3c00577. eCollection , 2024 May 27. PMID:38818051[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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