View source for 6c48


==Crystal structure of B-Myb-LIN9-LIN52 complex==
<StructureSection load='6c48' size='340' side='right'caption='[[6c48]], [[Resolution|resolution]] 2.32&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6c48]] is a 6 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=6C48 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6C48 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]] 2.32&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=6c48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c48 OCA], [https://pdbe.org/6c48 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6c48 RCSB], [https://www.ebi.ac.uk/pdbsum/6c48 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6c48 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/LIN9_HUMAN LIN9_HUMAN] Acts as a tumor suppressor. Inhibits DNA synthesis. Its ability to inhibit oncogenic transformation is mediated through its association with RB1. Plays a role in the expression of genes required for the G1/S transition.<ref>PMID:15538385</ref> <ref>PMID:16730350</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The MuvB transcriptional regulatory complex, which controls cell-cycle-dependent gene expression, cooperates with B-Myb to activate genes required for the G2 and M phases of the cell cycle. We have identified the domain in B-Myb that is essential for the assembly of the Myb-MuvB (MMB) complex. We determined a crystal structure that reveals how this B-Myb domain binds MuvB through the adaptor protein LIN52 and the scaffold protein LIN9. The structure and biochemical analysis provide an understanding of how oncogenic B-Myb is recruited to regulate genes required for cell-cycle progression, and the MMB interface presents a potential therapeutic target to inhibit cancer cell proliferation.

Structural mechanism of Myb-MuvB assembly.,Guiley KZ, Iness AN, Saini S, Tripathi S, Lipsick JS, Litovchick L, Rubin SM Proc Natl Acad Sci U S A. 2018 Sep 17. pii: 1808136115. doi:, 10.1073/pnas.1808136115. PMID:30224471<ref>PMID:30224471</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6c48" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Guiley KZ]]
[[Category: Rubin SM]]
[[Category: Tripathi SM]]