6e9g: Difference between revisions

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-'''Unreleased structure'''
-The entry 6e9g is ON HOLD  until Paper Publication
+==The crystal structure of bovine ultralong antibody BOV-2==
+<StructureSection load='6e9g' size='340' side='right'caption='[[6e9g]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6e9g]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6E9G OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6E9G FirstGlance]. <br>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6e9g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6e9g OCA], [http://pdbe.org/6e9g PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6e9g RCSB], [http://www.ebi.ac.uk/pdbsum/6e9g PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6e9g ProSAT]</span></td></tr>
+</table>
+<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.
-Authors: Dong, J., Crowe, J.E.
+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>
-Description: The crystal structure of bovine ultralong antibody BOV-2
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Crowe, J.E]]
+<div class="pdbe-citations 6e9g" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Crowe, J E]]
 [[Category: Dong, J]]
+[[Category: Antibody]]
+[[Category: Antibody diversity]]
+[[Category: Antigen-antibody reaction]]
+[[Category: B-lymphocyte]]
+[[Category: Bos taurus]]
+[[Category: Immune system]]
+[[Category: Monoclonal]]