9klt: Difference between revisions

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'''Unreleased structure'''


The entry 9klt is ON HOLD  until 2027-05-15
==Crystal structure of a Streptococcal protein G B1 mutant==
<StructureSection load='9klt' size='340' side='right'caption='[[9klt]], [[Resolution|resolution]] 2.88&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9klt]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Finegoldia_magna Finegoldia magna]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9KLT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9KLT 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]] 2.88&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</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=9klt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9klt OCA], [https://pdbe.org/9klt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9klt RCSB], [https://www.ebi.ac.uk/pdbsum/9klt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9klt ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q53291_FINMA Q53291_FINMA]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Homobivalent small binders represent bioactive dimeric proteins constructed by linking nanobodies or other small binders. As binding domain orientation in these dimeric binders affects binding affinity, expanding the orientation regulation techniques is crucial for optimizing their performance. Here, we report a 3D domain-swapping design as a genetic engineering approach to regulate the orientation of homobivalent small binders. We aimed to regulate B1 domain orientation of protein G as a model binder. By inserting single cysteine-containing polyproline sequences into loops located at the C- and N-terminal sides of the tertiary structure, we successfully designed 3D domain-swapped dimers with tail-to-tail and head-to-head orientations. Notably, the head-to-head-oriented dimer demonstrated potential as a functional homobivalent small binder. Our results highlight the applicability of the 3D domain-swapping design for regulating the orientation of homobivalent small binders and establish a foundation for developing 3D domain-swapped dimers.


Authors:  
Regulating the orientation of homobivalent small binders through 3D domain-swapping design.,Shiga S, Watanabe H, Makabe K, Honda S J Biol Chem. 2025 Dec 13;302(2):111053. doi: 10.1016/j.jbc.2025.111053. PMID:41391770<ref>PMID:41391770</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 9klt" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Finegoldia magna]]
[[Category: Large Structures]]
[[Category: Honda S]]
[[Category: Shiga S]]
[[Category: Watanabe H]]
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