6e8v: Difference between revisions
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The | ==The crystal structure of bovine ultralong antibody BOV-1== | ||
<StructureSection load='6e8v' size='340' side='right'caption='[[6e8v]], [[Resolution|resolution]] 3.79Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6e8v]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E8V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6E8V 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]] 3.79Å</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=6e8v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e8v OCA], [https://pdbe.org/6e8v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6e8v RCSB], [https://www.ebi.ac.uk/pdbsum/6e8v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6e8v ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/Q3T101_BOVIN Q3T101_BOVIN] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Antigen recognition by mammalian antibodies represents the most diverse setting for protein-protein interactions, because antibody variable regions contain exceptionally diverse variable gene repertoires of DNA sequences containing combinatorial, non-templated junctional mutational diversity. Some animals use additional strategies to achieve structural complexity in the antibody combining site, and one of the most interesting of these is the formation of ultralong heavy chain complementarity determining region 3 loops in cattle. Repertoire sequencing studies of bovine antibody heavy chain variable sequences revealed that bovine antibodies can contain heavy chain complementarity determining region 3 (CDRH3) loops with 60 or more amino acids, with complex structures stabilized by multiple disulfide bonds. It is clear that bovine antibodies can achieve long, peculiarly structured CDR3s, but the range of diversity and complexity of those structures is poorly understood. We determined the atomic resolution structure of seven ultralong bovine CDRH3 loops. The studies, combined with five previous structures, reveal a large diversity of cysteine pairing variations, and highly diverse globular domains. | |||
Structural Diversity of Ultralong CDRH3s in Seven Bovine Antibody Heavy Chains.,Dong J, Finn JA, Larsen PA, Smith TPL, Crowe JE Jr Front Immunol. 2019 Mar 22;10:558. doi: 10.3389/fimmu.2019.00558. eCollection, 2019. PMID:30967877<ref>PMID:30967877</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6e8v" style="background-color:#fffaf0;"></div> | ||
[[Category: | |||
==See Also== | |||
*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]] | |||
*[[Sandbox 20009|Sandbox 20009]] | |||
*[[3D structures of non-human antibody|3D structures of non-human antibody]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bos taurus]] | |||
[[Category: Large Structures]] | |||
[[Category: Crowe JE]] | |||
[[Category: Dong J]] | |||
Latest revision as of 15:34, 6 November 2024
The crystal structure of bovine ultralong antibody BOV-1The crystal structure of bovine ultralong antibody BOV-1
Structural highlights
FunctionPublication Abstract from PubMedAntigen recognition by mammalian antibodies represents the most diverse setting for protein-protein interactions, because antibody variable regions contain exceptionally diverse variable gene repertoires of DNA sequences containing combinatorial, non-templated junctional mutational diversity. Some animals use additional strategies to achieve structural complexity in the antibody combining site, and one of the most interesting of these is the formation of ultralong heavy chain complementarity determining region 3 loops in cattle. Repertoire sequencing studies of bovine antibody heavy chain variable sequences revealed that bovine antibodies can contain heavy chain complementarity determining region 3 (CDRH3) loops with 60 or more amino acids, with complex structures stabilized by multiple disulfide bonds. It is clear that bovine antibodies can achieve long, peculiarly structured CDR3s, but the range of diversity and complexity of those structures is poorly understood. We determined the atomic resolution structure of seven ultralong bovine CDRH3 loops. The studies, combined with five previous structures, reveal a large diversity of cysteine pairing variations, and highly diverse globular domains. Structural Diversity of Ultralong CDRH3s in Seven Bovine Antibody Heavy Chains.,Dong J, Finn JA, Larsen PA, Smith TPL, Crowe JE Jr Front Immunol. 2019 Mar 22;10:558. doi: 10.3389/fimmu.2019.00558. eCollection, 2019. PMID:30967877[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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