7qts: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7qts]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_sp. Streptococcus sp.]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QTS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QTS FirstGlance]. <br>
<table><tr><td colspan='2'>[[7qts]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_sp. Streptococcus sp.]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QTS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QTS FirstGlance]. <br>
</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=7qts FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qts OCA], [https://pdbe.org/7qts PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qts RCSB], [https://www.ebi.ac.uk/pdbsum/7qts PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qts ProSAT]</span></td></tr>
</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=7qts FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qts OCA], [https://pdbe.org/7qts PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qts RCSB], [https://www.ebi.ac.uk/pdbsum/7qts PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qts ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/SPG1_STRSG SPG1_STRSG] Binds to the constant Fc region of IgG with high affinity.
[https://www.uniprot.org/uniprot/SPG1_STRSG SPG1_STRSG] Binds to the constant Fc region of IgG with high affinity.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Most experimental methods for structural biology proceed in vitro and therefore the contribution of the intracellular environment on protein structure and dynamics is absent. Studying proteins at atomic resolution in living mammalian cells has been elusive due to the lack of methodologies. In-cell nuclear magnetic resonance spectroscopy (in-cell NMR) is an emerging technique with the power to do so. Here, we improved current methods of in-cell NMR by the development of a reporter system that allows monitoring the delivery of exogenous proteins into mammalian cells, a process that we called here "transexpression". The reporter system was used to develop an efficient protocol for in-cell NMR which enables spectral acquisition with higher quality for both disordered and folded proteins. With this method, the 3D atomic resolution structure of the model protein GB1 in human cells was determined with a backbone root-mean-square deviation (RMSD) of 1.1 A.
Protein structure determination in human cells by in-cell NMR and a reporter system to optimize protein delivery or transexpression.,Gerez JA, Prymaczok NC, Kadavath H, Ghosh D, Butikofer M, Fleischmann Y, Guntert P, Riek R Commun Biol. 2022 Dec 2;5(1):1322. doi: 10.1038/s42003-022-04251-6. PMID:36460747<ref>PMID:36460747</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7qts" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Latest revision as of 06:18, 19 June 2024

GB1 in mammalian cells, 10 uM

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