8vu6: Difference between revisions
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==Wheat Germ Agglutinin (WGA) domain A== | |||
<StructureSection load='8vu6' size='340' side='right'caption='[[8vu6]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[8vu6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Triticum_aestivum Triticum aestivum]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8VU6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8VU6 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=8vu6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8vu6 OCA], [https://pdbe.org/8vu6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8vu6 RCSB], [https://www.ebi.ac.uk/pdbsum/8vu6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8vu6 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/AGI1_WHEAT AGI1_WHEAT] N-acetyl-D-glucosamine / N-acetyl-D-neuraminic acid binding lectin. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Wheat germ agglutinin (WGA) demonstrates potential as an oral delivery agent owing to its selective binding to carbohydrates and its capacity to traverse biological membranes. In this study, we employed differential scanning calorimetry and molecular dynamics simulations to comprehensively characterize the thermal unfolding process of both the complete lectin and its four isolated domains. Furthermore, we present the nuclear magnetic resonance structures of three domains that were previously lacking experimental structures in their isolated forms. Our results provide a collective understanding of the energetic and structural factors governing the intricate unfolding mechanism of the complete agglutinin, shedding light on the specific role played by each domain in this process. The analysis revealed negligible interdomain cooperativity, highlighting instead significant coupling between dimer dissociation and the unfolding of the more labile domains. By comparing the dominant interactions, we rationalized the stability differences among the domains. Understanding the structural stability of WGA opens avenues for enhanced drug delivery strategies, underscoring its potential as a promising carrier throughout the gastrointestinal environment. | |||
Decoding the mechanism governing the structural stability of wheat germ agglutinin and its isolated domains: A combined calorimetric, NMR, and MD simulation study.,Medrano-Cerano JL, Cofas-Vargas LF, Leyva E, Rauda-Ceja JA, Calderon-Vargas M, Cano-Sanchez P, Titaux-Delgado G, Melchor-Meneses CM, Hernandez-Arana A, Del Rio-Portilla F, Garcia-Hernandez E Protein Sci. 2024 Jun;33(6):e5020. doi: 10.1002/pro.5020. PMID:38747397<ref>PMID:38747397</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 8vu6" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Triticum aestivum]] | |||
[[Category: Garcia-Hernandez E]] | |||
[[Category: Titaux-Delgado GA]] | |||
[[Category: Del Rio-Portilla F]] | |||
Revision as of 08:20, 5 June 2024
Wheat Germ Agglutinin (WGA) domain AWheat Germ Agglutinin (WGA) domain A
Structural highlights
FunctionAGI1_WHEAT N-acetyl-D-glucosamine / N-acetyl-D-neuraminic acid binding lectin. Publication Abstract from PubMedWheat germ agglutinin (WGA) demonstrates potential as an oral delivery agent owing to its selective binding to carbohydrates and its capacity to traverse biological membranes. In this study, we employed differential scanning calorimetry and molecular dynamics simulations to comprehensively characterize the thermal unfolding process of both the complete lectin and its four isolated domains. Furthermore, we present the nuclear magnetic resonance structures of three domains that were previously lacking experimental structures in their isolated forms. Our results provide a collective understanding of the energetic and structural factors governing the intricate unfolding mechanism of the complete agglutinin, shedding light on the specific role played by each domain in this process. The analysis revealed negligible interdomain cooperativity, highlighting instead significant coupling between dimer dissociation and the unfolding of the more labile domains. By comparing the dominant interactions, we rationalized the stability differences among the domains. Understanding the structural stability of WGA opens avenues for enhanced drug delivery strategies, underscoring its potential as a promising carrier throughout the gastrointestinal environment. Decoding the mechanism governing the structural stability of wheat germ agglutinin and its isolated domains: A combined calorimetric, NMR, and MD simulation study.,Medrano-Cerano JL, Cofas-Vargas LF, Leyva E, Rauda-Ceja JA, Calderon-Vargas M, Cano-Sanchez P, Titaux-Delgado G, Melchor-Meneses CM, Hernandez-Arana A, Del Rio-Portilla F, Garcia-Hernandez E Protein Sci. 2024 Jun;33(6):e5020. doi: 10.1002/pro.5020. PMID:38747397[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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