6c48
From Proteopedia
Crystal structure of B-Myb-LIN9-LIN52 complex
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] [MYBB_HUMAN] Transcription factor involved in the regulation of cell survival, proliferation, and differentiation. Transactivates the expression of the CLU gene.[3] Publication Abstract from PubMedThe 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[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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Categories: Human | Large Structures | Guiley, K Z | Rubin, S M | Tripathi, S M | B-myb | Cell cycle | Cell cycle-dna binding complex | Lin52 | Lin9 | Mmb | Muvb | Myb
