6l9d: Difference between revisions
Jump to navigation
Jump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==X-ray structure of synthetic GB1 domain with mutations K10(DVA), T11S== | ==X-ray structure of synthetic GB1 domain with mutations K10(DVA), T11S== | ||
<StructureSection load='6l9d' size='340' side='right'caption='[[6l9d]]' scene=''> | <StructureSection load='6l9d' size='340' side='right'caption='[[6l9d]], [[Resolution|resolution]] 1.73Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L9D OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6l9d]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6L9D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6L9D FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=DVA:D-VALINE'>DVA</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=6l9d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l9d OCA], [https://pdbe.org/6l9d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6l9d RCSB], [https://www.ebi.ac.uk/pdbsum/6l9d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6l9d 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 6l9d" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Protein G|Protein G]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Chatterjee J]] | [[Category: Chatterjee, J]] | ||
[[Category: Khatri B]] | [[Category: Khatri, B]] | ||
[[Category: Majumder P]] | [[Category: Majumder, P]] | ||
[[Category: Penmatsa A]] | [[Category: Penmatsa, A]] | ||
[[Category: D-aminoacid substitution]] | |||
[[Category: Immune system]] | |||
[[Category: Synthetic gb1 domain variant]] | |||
Revision as of 13:26, 4 August 2021
X-ray structure of synthetic GB1 domain with mutations K10(DVA), T11SX-ray structure of synthetic GB1 domain with mutations K10(DVA), T11S
Structural highlights
Function[SPG1_STRSG] Binds to the constant Fc region of IgG with high affinity. Publication Abstract from PubMedAbundant 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|
| ||||||||||||||||