9p6w: Difference between revisions

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'''Unreleased structure'''


The entry 9p6w is ON HOLD until Paper Publication
==Honey Truffle Active Component==
<StructureSection load='9p6w' size='340' side='right'caption='[[9p6w]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9p6w]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mattirolomyces_terfezioides Mattirolomyces terfezioides]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9P6W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9P6W FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, models</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=9p6w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9p6w OCA], [https://pdbe.org/9p6w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9p6w RCSB], [https://www.ebi.ac.uk/pdbsum/9p6w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9p6w ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Sweet proteins trigger sweet taste perception through interactions with the human T1R2/R3 sweet taste receptor. To date, relatively few proteins have been identified as causing sweet taste perception, and the four most studied proteins: monellin, brazzein, thaumatin, and honey truffle active component (HT-AC), have minimal sequence homology or structural similarities aside from positively charged surface sites. Sweet taste perception has also been found to be readily perturbed by minor changes in the protein structure, such as natural isoforms inherent to heterologous expression of the protein, and synthetic amino acid substitutions. This study uses ab initio rigid-body docking to predict the interactions of known sweet proteins and variants with a recently resolved cryo-EM structure of the T1R2/R3 sweet taste receptor, incorporating comparative analyses between apo-, holo-, and a potentially transient conformation of the receptor. HT-AC mediated activation of the sweet taste receptor is confirmed by in vitro cell-based assays, and results from in silico docking of various sweet proteins are used to derive additional insights regarding sweet taste perception. Perturbations of HT-AC due to naturally occurring post-translational modifications and synthetic modifications are evaluated using in vitro and in silico methods to determine robustness of the interaction between T1R2/R3 and sweet proteins with primary focuses on HT-AC.


Authors:  
Sweet Protein Allosteric Binding and Activation of the Human T1R2/R3 Sweet Receptor: A Simulation Model Validated by in Vitro Receptor Activation Assay.,Vo P, Connors DE, Sharkey BP, Gravina SA, Servant G, McFarland CT, Pitkanen TT, Burk CD, Cowen CP, Grein EM, Henderson SM, Langan JP, Rael LT, Totman RJ, Clark A, Guo Z, Han A, Meilen J, Nadal M, Westgate A, Williams ME, Zhang L, Patnaik R Biochemistry. 2026 Feb 17;65(4):399-416. doi: 10.1021/acs.biochem.5c00622. Epub , 2026 Jan 27. PMID:41591896<ref>PMID:41591896</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 9p6w" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mattirolomyces terfezioides]]
[[Category: Connors DE]]
[[Category: McFarland CT]]

Latest revision as of 06:28, 22 April 2026

Honey Truffle Active Component

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