5drx: Difference between revisions

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New page: '''Unreleased structure''' The entry 5drx is ON HOLD until Paper Publication Authors: Minici, C., Degano, M. Description: Crystal structure of the BCR Fab fragment from subset #4 case ...
 
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'''Unreleased structure'''


The entry 5drx is ON HOLD  until Paper Publication
==Crystal structure of the BCR Fab fragment from subset #4 case CLL240==
<StructureSection load='5drx' size='340' side='right'caption='[[5drx]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5drx]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5DRX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5DRX 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]] 2.104&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</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=5drx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5drx OCA], [https://pdbe.org/5drx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5drx RCSB], [https://www.ebi.ac.uk/pdbsum/5drx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5drx ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Cell-autonomous B-cell receptor (BcR)-mediated signalling is a hallmark feature of the neoplastic B lymphocytes in chronic lymphocytic leukaemia (CLL). Here we elucidate the structural basis of autonomous activation of CLL B cells, showing that BcR immunoglobulins initiate intracellular signalling through homotypic interactions between epitopes that are specific for each subgroup of patients with homogeneous clinicobiological profiles. The molecular details of the BcR-BcR interactions apparently dictate the clinical course of disease, with stronger affinities and longer half-lives in indolent cases, and weaker, short-lived contacts mediating the aggressive ones. The diversity of homotypic BcR contacts leading to cell-autonomous signalling reconciles the existence of a shared pathogenic mechanism with the biological and clinical heterogeneity of CLL and offers opportunities for innovative treatment strategies.


Authors: Minici, C., Degano, M.
Distinct homotypic B-cell receptor interactions shape the outcome of chronic lymphocytic leukaemia.,Minici C, Gounari M, Ubelhart R, Scarfo L, Duhren-von Minden M, Schneider D, Tasdogan A, Alkhatib A, Agathangelidis A, Ntoufa S, Chiorazzi N, Jumaa H, Stamatopoulos K, Ghia P, Degano M Nat Commun. 2017 Jun 9;8:15746. doi: 10.1038/ncomms15746. PMID:28598442<ref>PMID:28598442</ref>


Description: Crystal structure of the BCR Fab fragment from subset #4 case CLL240
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Minici, C]]
<div class="pdbe-citations 5drx" style="background-color:#fffaf0;"></div>
[[Category: Degano, M]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Degano M]]
[[Category: Minici C]]
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