6C48
Crystal structure of B-Myb-LIN9-LIN52 complex
Summary for 6C48
| Entry DOI | 10.2210/pdb6c48/pdb |
| Descriptor | Protein lin-9 homolog, Myb-related protein B, Protein lin-52 homolog, ... (5 entities in total) |
| Functional Keywords | myb, b-myb, lin52, lin9, mmb, muvb, cell cycle, cell cycle-dna binding complex, cell cycle/dna binding |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 6 |
| Total formula weight | 51136.46 |
| Authors | Guiley, K.Z.,Tripathi, S.M.,Rubin, S.M. (deposition date: 2018-01-11, release date: 2018-09-19, Last modification date: 2019-12-04) |
| Primary citation | Guiley, K.Z.,Iness, A.N.,Saini, S.,Tripathi, S.,Lipsick, J.S.,Litovchick, L.,Rubin, S.M. Structural mechanism of Myb-MuvB assembly. Proc. Natl. Acad. Sci. U.S.A., 115:10016-10021, 2018 Cited by PubMed Abstract: 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. PubMed: 30224471DOI: 10.1073/pnas.1808136115 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.32 Å) |
Structure validation
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