Target Name: MED7
NCBI ID: G9443
Review Report on MED7 Target / Biomarker Content of Review Report on MED7 Target / Biomarker
MED7
Other Name(s): Transcriptional coactivator CRSP33 | OTTHUMP00000160735 | Cofactor required for Sp1 transcriptional activation subunit 9 | Cofactor required for Sp1 transcriptional activation, subunit 9, 33kDa | transcriptional coactivator CRSP33 | cofactor required for Sp1 transcriptional activation, subunit 9 (33kD) | Cofactor required for Sp1 transcriptional activation, subunit 9 (33kD) | hMED7 | CRSP33 | Mediator of RNA polymerase II transcription subunit 7 | Mediator complex subunit 7, transcript variant 1 | MGC12284 | MED7 variant 1 | CRSP complex subunit 9 | CRSP9 | cofactor required for Sp1 transcriptional activation subunit 9 | Activator-recruited cofactor 34 kDa component | Mediator complex subunit 7 | MED7_HUMAN | cofactor required for Sp1 transcriptional activation, subunit 9, 33kDa | activator-recruited cofactor 34 kDa component | RNA polymerase transcriptional regulation mediator subunit 7 homolog | mediator complex subunit 7 | ARC34

MED7: A Transcription Factor for Cellular Processes and A Promising Drug Target

MED7 (Transcriptional coactivator CRSP33) is a protein that plays a crucial role in the regulation of gene expression in various organisms, including humans. It belongs to the CRSP family of transcription factors, which are known for their ability to promote the recruitment of coactivators to their DNA-binding sites. MED7 has been shown to play a key role in the regulation of cell proliferation, differentiation, and survival, and is thus a promising drug target in various diseases.

Structure and Function

The CRSP family of transcription factors consists of six subfamilies, including CRSP1-CRSP6. These subfamilies are characterized by the presence of a specific domain, known as the coactivator-binding site, which is responsible for the recruitment of coactivators to the DNA-binding site . The coactivator is a protein that can interact with the transcription factor to either enhance or inhibit its activity.

MED7 is a member of the CRSP3 family, which consists of three subfamilies: CRSP3, CRSP3a, and CRSP3b. These subfamilies share a similar structure and function, with the exception of the presence or absence of a specific domain, known as the N-terminal hypervariable region (HVR1), and the number and arrangement of the coactivator-binding sites.

MED7 has a characteristic molecular weight of 19 kDa and a calculated pI of 1.95. It consists of a unique N-terminal region that contains a single domain, known as the coactivator-binding site, and a C-terminal region that contains a hinge- like structure. The coactivator-binding site is responsible for the recruitment of coactivators, and is composed of a unique amino acid sequence that consists of a putative alpha-helic acid loop and a hydrophobic alanine-rich region.

The function of MED7 is closely linked to its ability to recruit coactivators to its DNA-binding site. Coactivators can either enhance or inhibit the activity of MED7, depending on the specific context. For example, when MED7 is coactivated with the transcription factor p53, it enhances the transcriptional activity of target genes. On the other hand, when MED7 is coactivated with the transcription factor NF-kappa-B, it inhibits the transcriptional activity of target genes.

MED7 has been shown to play a key role in the regulation of various cellular processes, including cell proliferation, differentiation, and survival. For example, it has been shown to be involved in the regulation of cell cycle progression, with studies showing that it promotes the G1 phase and inhibits the S-phase. It has also been shown to be involved in the regulation of cell survival, with studies showing that it promotes the survival of cancer cells and inhibits the survival of normal cells.

Drug Targeting

MED7 is a promising drug target due to its involvement in various cellular processes that are often disrupted in diseases, such as cancer. Several studies have shown that inhibiting the activity of MED7 can lead to the inhibition of various cellular processes, including cell proliferation, differentiation , and survival.

One of the most promising strategies for targeting MED7 is the use of small molecules that can inhibit the activity of the coactivators that interact with MED7. These small molecules can either be derived from natural compounds or synthesized using a variety of techniques. For example, several studies have shown that inhibitors of the coactivators that interact with MED7, such as the DNA-binding proteins p53 and NF-kappa-B, can lead to the inhibition of cellular processes, such as cell proliferation and survival.

Another strategy for targeting MED7 is the use of antibodies that can specifically recognize and interact with the coactivator-binding site of MED7. These antibodies can be used to either enhance or inhibit the activity of MED7, depending on the specific context. For example, studies have shown that antibodies that can specifically recognize and interact with the coactivator-binding site of MED7 can lead to the inhibition of cellular processes, such as

Protein Name: Mediator Complex Subunit 7

Functions: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors

The "MED7 Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about MED7 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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MED8 | MED9 | MEDAG | Mediator Complex | Mediator of RNA Polymerase II Transcription | MEF2A | MEF2B | MEF2C | MEF2C-AS1 | MEF2C-AS2 | MEF2D | MEFV | MEG3 | MEG8 | MEG9 | MEGF10 | MEGF11 | MEGF6 | MEGF8 | MEGF9 | MEI1 | MEI4 | MEIG1 | MEIKIN | MEIOB | MEIOC | MEIOSIN | MEIS1 | MEIS1-AS2 | MEIS1-AS3 | MEIS2 | MEIS3 | MEIS3P1 | MEIS3P2 | Melanin | Melanin-concentrating hormone (MCH) receptor | Melanocortin receptor | Melanoma-Associated Antigen | Melatonin receptor | MELK | MELTF | MELTF-AS1 | Membrane-Bound Protein Tyrosine Phosphatases (rPTPs) | Membrane-spanning 4-domains subfamily A member 4A | MEMO1 | MEMO1P1 | MEMO1P4 | MEMO1P5 | MEN1 | MEOX1 | MEOX2 | MEP1A | MEP1AP2 | MEP1AP4 | MEP1B | MEPCE | MEPE | MERTK | MESD | MESP1 | MESP2 | MEST | MESTIT1 | MESTP3 | MESTP4 | MET | Metabotropic glutamate (mGluR) receptor | Metallothionein | METAP1 | METAP1D | METAP2 | Metaxin complex | Methionine adenosyltransferase | Methionine adenosyltransferase II | Methionyl aminopeptidase | Methylcytosine dioxygenase (TET) | METRN | METRNL | METTL1 | METTL13 | METTL14 | METTL15 | METTL15P1 | METTL15P2 | METTL16 | METTL17 | METTL18 | METTL21A | METTL21C | METTL21EP | METTL22 | METTL23 | METTL24 | METTL25 | METTL25B | METTL26 | METTL27 | METTL2A | METTL2B | METTL3