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| | ==Crystal structure of B-Myb-LIN9-LIN52 complex== | | ==Crystal structure of B-Myb-LIN9-LIN52 complex== |
| - | <StructureSection load='6c48' size='340' side='right' caption='[[6c48]], [[Resolution|resolution]] 2.32Å' scene=''> | + | <StructureSection load='6c48' size='340' side='right'caption='[[6c48]], [[Resolution|resolution]] 2.32Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6c48]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6C48 FirstGlance]. <br> | + | <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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.32Å</td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LIN9, BARA, TGS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), MYBL2, BMYB ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), LIN52, C14orf46 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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> |
| - | <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=6c48 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6c48 OCA], [http://pdbe.org/6c48 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6c48 RCSB], [http://www.ebi.ac.uk/pdbsum/6c48 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6c48 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> [[http://www.uniprot.org/uniprot/MYBB_HUMAN MYBB_HUMAN]] Transcription factor involved in the regulation of cell survival, proliferation, and differentiation. Transactivates the expression of the CLU gene.<ref>PMID:10770937</ref> | + | [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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Guiley, K Z]] | + | [[Category: Large Structures]] |
| - | [[Category: Rubin, S M]] | + | [[Category: Guiley KZ]] |
| - | [[Category: Tripathi, S M]] | + | [[Category: Rubin SM]] |
| - | [[Category: B-myb]] | + | [[Category: Tripathi SM]] |
| - | [[Category: Cell cycle]]
| + | |
| - | [[Category: Cell cycle-dna binding complex]]
| + | |
| - | [[Category: Lin52]]
| + | |
| - | [[Category: Lin9]]
| + | |
| - | [[Category: Mmb]]
| + | |
| - | [[Category: Muvb]]
| + | |
| - | [[Category: Myb]]
| + | |
| Structural highlights
Function
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.[1] [2]
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gagrica S, Hauser S, Kolfschoten I, Osterloh L, Agami R, Gaubatz S. Inhibition of oncogenic transformation by mammalian Lin-9, a pRB-associated protein. EMBO J. 2004 Nov 24;23(23):4627-38. Epub 2004 Nov 11. PMID:15538385 doi:http://dx.doi.org/7600470
- ↑ Sandoval R, Xue J, Tian X, Barrett K, Pilkinton M, Ucker DS, Raychaudhuri P, Kineman RD, Luque RM, Baida G, Zou X, Valli VE, Cook JL, Kiyokawa H, Colamonici OR. A mutant allele of BARA/LIN-9 rescues the cdk4-/- phenotype by releasing the repression on E2F-regulated genes. Exp Cell Res. 2006 Aug 1;312(13):2465-75. Epub 2006 Apr 25. PMID:16730350 doi:http://dx.doi.org/S0014-4827(06)00156-X
- ↑ Guiley KZ, Iness AN, Saini S, Tripathi S, Lipsick JS, Litovchick L, Rubin SM. Structural mechanism of Myb-MuvB assembly. Proc Natl Acad Sci U S A. 2018 Sep 17. pii: 1808136115. doi:, 10.1073/pnas.1808136115. PMID:30224471 doi:http://dx.doi.org/10.1073/pnas.1808136115
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