9vx2: Difference between revisions

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'''Unreleased structure'''


The entry 9vx2 is ON HOLD  until Paper Publication
==Crystal structure of the apo form of HisMab-1 Fab==
<StructureSection load='9vx2' size='340' side='right'caption='[[9vx2]], [[Resolution|resolution]] 2.39&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9vx2]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9VX2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9VX2 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]] 2.39&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=9vx2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9vx2 OCA], [https://pdbe.org/9vx2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9vx2 RCSB], [https://www.ebi.ac.uk/pdbsum/9vx2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9vx2 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The polyhistidine tag (His-tag) is one of the most widely used peptide tags for the purification of recombinant proteins, owing to its compatibility with immobilized metal affinity chromatography. While numerous anti-His-tag antibodies are commercially available, their quantitative affinity data and structural insights are limited. Here, we present a detailed physicochemical and structural characterization of a novel anti-His-tag antibody, HisMab-1. Isothermal titration calorimetry showed that the Fab fragment of HisMab-1 binds to a hexahistidine peptide in an enthalpy-driven manner, with a dissociation constant (K(D)) of approximately 30 nM at a neutral pH. The crystal structure of the HisMab-1-hexahistidine peptide complex at 2.39-A resolution revealed that HisMab-1 primarily recognizes the first, second, fourth, and fifth histidine residues of the peptide through multiple interactions, including hydrogen bonding and pi-pi stacking, which collectively contribute to the high specificity of the antibody. Notably, HisMab-1 also binds to a His-tag embedded within a conformationally constrained beta-hairpin loop without reducing affinity, highlighting its structural adaptability. These findings establish HisMab-1 as a high-affinity, high-specificity, structurally validated anti-His-tag antibody with broad potential in diverse protein engineering and structural biology applications.


Authors:  
Functional and Structural Characterization of a Novel Anti-His-tag Antibody, HisMab-1.,Hitomi N, Hoshi S, Kaneko MK, Kato R, Iwasaki K, Takagi J, Kato Y, Harada-Hikita A, Arimori T J Mol Biol. 2025 Dec 3;438(2):169574. doi: 10.1016/j.jmb.2025.169574. PMID:41349762<ref>PMID:41349762</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 9vx2" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Arimori T]]
[[Category: Harada-Hikita A]]
[[Category: Hoshi S]]
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