6l91
From Proteopedia
(Difference between revisions)
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| - | ==X-ray structure of synthetic GB1 domain with the mutation K10(DVA) | + | ==X-ray structure of synthetic GB1 domain with the mutation K10(DVA)== |
<StructureSection load='6l91' size='340' side='right'caption='[[6l91]], [[Resolution|resolution]] 1.84Å' scene=''> | <StructureSection load='6l91' size='340' side='right'caption='[[6l91]], [[Resolution|resolution]] 1.84Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L91 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6L91 FirstGlance]. <br> |
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.842Å</td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.842Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DVA:D-VALINE'>DVA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DVA:D-VALINE'>DVA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=6l91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l91 OCA], [https://pdbe.org/6l91 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6l91 RCSB], [https://www.ebi.ac.uk/pdbsum/6l91 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6l91 ProSAT]</span></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=6l91 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l91 OCA], [https://pdbe.org/6l91 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6l91 RCSB], [https://www.ebi.ac.uk/pdbsum/6l91 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6l91 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| - | == Function == | ||
| - | [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 == | ||
| - | Abundant n --> pi* interactions between adjacent backbone carbonyl groups, identified by statistical analysis of protein structures, are predicted to play an important role in dictating the structure of proteins. However, experimentally testing the prediction in proteins has been challenging due to the weak nature of this interaction. By amplifying the strength of the n --> pi* interaction via amino acid substitution and thioamide incorporation at a solvent exposed beta-turn within the GB1 proteins and Pin 1 WW domain, we demonstrate that an n --> pi* interaction increases the structural stability of proteins by restricting the varphi torsion angle. Our results also suggest that amino acid side-chain identity and its rotameric conformation play an important and decisive role in dictating the strength of an n --> pi* interaction. | ||
| - | |||
| - | Increasing protein stability by engineering the n --> pi* interaction at the beta-turn.,Khatri B, Majumder P, Nagesh J, Penmatsa A, Chatterjee J Chem Sci. 2020 Jul 30;11(35):9480-9487. doi: 10.1039/d0sc03060k. PMID:34094214<ref>PMID:34094214</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 6l91" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Protein G|Protein G]] | *[[Protein G|Protein G]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Streptococcus sp. 'group G']] | ||
[[Category: Chatterjee J]] | [[Category: Chatterjee J]] | ||
[[Category: Khatri B]] | [[Category: Khatri B]] | ||
[[Category: Majumder P]] | [[Category: Majumder P]] | ||
[[Category: Penmatsa A]] | [[Category: Penmatsa A]] | ||
Current revision
X-ray structure of synthetic GB1 domain with the mutation K10(DVA)
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