7wso: Difference between revisions

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~~'''Unreleased structure'''~~

~~The entry~~ 7wso is ~~ON HOLD until Paper~~ Publication

==Structure of a membrane protein G==

== Structural highlights ==

<table><tr><td colspan='2'>[[7wso]] 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=7WSO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WSO FirstGlance]. <br>

</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=7wso FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wso OCA], [https://pdbe.org/7wso PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wso RCSB], [https://www.ebi.ac.uk/pdbsum/7wso PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wso ProSAT]</span></td></tr>

</table>

== Function ==

[[https://www.uniprot.org/uniprot/A0A0A0MS08_HUMAN A0A0A0MS08_HUMAN]]

== Publication Abstract from PubMed ==

The B cell receptor (BCR) complex plays a critical role in B cell development and immune responses. The assembly mechanisms underlying the BCR complex remain unknown. We determined the cryo-electron microscopy (cryo-EM) structures of human IgG-BCR and IgM-BCR, which consist of membrane-bound immunoglobulin molecules (mIg) and Igalpha/beta subunits at a 1:1 stoichiometry. Assembly of both BCR complexes involves their extracellular domains, membrane-proximal connection peptides, and transmembrane (TM) helices. The TM helices of mIgG and mIgM share a conserved set of hydrophobic and polar interactions with Igalpha/beta TM helices. By contrast, the IgG-Cgamma3 and IgM-Cmu4 domains interact with extracellular Ig-like domains of Igalpha/beta through head-to-tail and side-by-side modes, respectively. This work reveals the structural basis for BCR assembly and provides insights into BCR triggering.

~~Authors~~:

Cryo-EM structures of two human B cell receptor isotypes.,Ma X, Zhu Y, Dong, Chen Y, Wang S, Yang D, Ma Z, Zhang A, Zhang F, Guo C, Huang Z Science. 2022 Aug 19;377(6608):880-885. doi: 10.1126/science.abo3828. Epub 2022, Aug 18. PMID:35981028<ref>PMID:35981028</ref>

~~Description~~:

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased~~ Structures]]

</div>

== References ==

__TOC__

</StructureSection>

[[Category: Homo sapiens]]

[[Category: Large Structures]]

[[Category: Chen Y]]

[[Category: Huang Z]]

[[Category: Ma X]]

[[Category: Zhu Y]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 7wso is ON HOLD  until Paper Publication
+==Structure of a membrane protein G==
+<StructureSection load='7wso' size='340' side='right'caption='[[7wso]], [[Resolution|resolution]] 3.03&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[7wso]] 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=7WSO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7WSO FirstGlance]. <br>
+</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=7wso FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7wso OCA], [https://pdbe.org/7wso PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7wso RCSB], [https://www.ebi.ac.uk/pdbsum/7wso PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7wso ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[https://www.uniprot.org/uniprot/A0A0A0MS08_HUMAN A0A0A0MS08_HUMAN]]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The B cell receptor (BCR) complex plays a critical role in B cell development and immune responses. The assembly mechanisms underlying the BCR complex remain unknown. We determined the cryo-electron microscopy (cryo-EM) structures of human IgG-BCR and IgM-BCR, which consist of membrane-bound immunoglobulin molecules (mIg) and Igalpha/beta subunits at a 1:1 stoichiometry. Assembly of both BCR complexes involves their extracellular domains, membrane-proximal connection peptides, and transmembrane (TM) helices. The TM helices of mIgG and mIgM share a conserved set of hydrophobic and polar interactions with Igalpha/beta TM helices. By contrast, the IgG-Cgamma3 and IgM-Cmu4 domains interact with extracellular Ig-like domains of Igalpha/beta through head-to-tail and side-by-side modes, respectively. This work reveals the structural basis for BCR assembly and provides insights into BCR triggering.
-Authors:
+Cryo-EM structures of two human B cell receptor isotypes.,Ma X, Zhu Y, Dong, Chen Y, Wang S, Yang D, Ma Z, Zhang A, Zhang F, Guo C, Huang Z Science. 2022 Aug 19;377(6608):880-885. doi: 10.1126/science.abo3828. Epub 2022, Aug 18. PMID:35981028<ref>PMID:35981028</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 7wso" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Chen Y]]
+[[Category: Huang Z]]
+[[Category: Ma X]]
+[[Category: Zhu Y]]