4hgm: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4hgm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Squalus_acanthias Squalus acanthias]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HGM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HGM FirstGlance]. <br>
<table><tr><td colspan='2'>[[4hgm]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Squalus_acanthias Squalus acanthias]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HGM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HGM FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></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]] 2.34&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</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=4hgm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hgm OCA], [https://pdbe.org/4hgm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hgm RCSB], [https://www.ebi.ac.uk/pdbsum/4hgm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hgm 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=4hgm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hgm OCA], [https://pdbe.org/4hgm PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hgm RCSB], [https://www.ebi.ac.uk/pdbsum/4hgm PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hgm ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
== Function ==
[https://www.uniprot.org/uniprot/ALBU_HUMAN ALBU_HUMAN] Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc.<ref>PMID:19021548</ref>  
[https://www.uniprot.org/uniprot/ALBU_HUMAN ALBU_HUMAN] Serum albumin, the main protein of plasma, has a good binding capacity for water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc.<ref>PMID:19021548</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The immunoglobulin new antigen receptors (IgNARs) are a class of Ig-like molecules of the shark immune system that exist as heavy chain-only homodimers and bind antigens by their single-domain variable regions (V-NARs). Following shark immunization and/or in vitro selection, V-NARs can be generated as soluble, stable and specific high-affinity monomeric binding proteins of ~12 kDa. We have previously isolated a V-NAR from an immunized spiny dogfish shark, named E06, which binds specifically and with high affinity to human, mouse and rat serum albumins. Humanization of E06 was carried out by converting over 60% of non-CDR residues to that of a human germline Vkappa1 sequence, DPK9. The resulting huE06 molecules have largely retained the specificity and affinity of antigen binding of the parental V-NAR. Crystal structures of the shark E06 and its humanized variant (huE06 v1.1), in complex with HSA, were determined at 3A and 2.3A resolution, respectively. The huE06 v1.1 molecule retained all but one amino acid residues involved in the binding site for HSA. Structural analysis of these V-NARs has revealed an unusual variable domain-antigen interaction. E06 interacts with HSA in an atypical mode that utilizes extensive framework contacts in addition to CDRs, that has not been previously seen in V-NARs. On the basis of the structure, the roles of various elements of the molecule are described with respect to antigen binding and V-NAR stability. This information broadens the general understanding of antigen recognition and provides a framework for further design and humanization of shark IgNARs.
Atypical Antigen Recognition Mode of a Shark IgNAR Variable Domain Characterized by Humanization and Structural Analysis.,Kovalenko OV, Olland A, Piche-Nicholas N, Godbole A, King D, Svenson K, Calabro V, Muller MR, Barelle CJ, Somers W, Gill DS, Mosyak L, Tchistiakova L J Biol Chem. 2013 Apr 30. PMID:23632026<ref>PMID:23632026</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4hgm" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==

Latest revision as of 12:14, 6 March 2024

Shark IgNAR Variable Domain

4hgm, resolution 2.34Å

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