3079093-16-3
Chemical Structure
MMH1
- CAS No.: 3079093-16-3
- Formula:C26H29N5O3S
- Molecular Weight:491.61
InChIKey: AEEGEVCKDJFBRN-IBGZPJMESA-N
SMILES: CC1=C(C)SC2=C1C(C3=CC=C(NC(C=C)=O)C=C3)=N[C@@H](CC(OC(C)(C)C)=O)C4=NN=C(C)N42
Biological Activity: MMH1 is a novel BRD4 molecular glue degrader. MMH1 functions by recruiting the CUL4 DCAF16 ligase to the second bromodomain of BRD4 (BRD4 BD2). MMH1 binds to the JQ1-binding site of BRD4 BD2, acts as a template to covalently modify Cys58 of DCAF16, stabilizes the BRD4-DCAF16 ternary complex, and thereby promotes BRD4 degradation via the CRL4DCAF16 ubiquitin ligase pathway. Using BRD4 BD2 as a structural template, MMH1 covalently modifies Cys87 of GAK and induces the GAK-BRD4 BD2 interaction. Through its covalent mechanism, MMH1 exhibits sustained BRD4 degradation activity, and shows selective degradation activity for BRD4 BD2 over BRD4 BD1[1].
| Cat. No. | Product Name | Purity | Description | Pricing | |||||||||||||||||||
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MMH1 | 99.83% | MMH1 is a novel BRD4 molecular glue degrader. MMH1 functions by recruiting the CUL4 DCAF16 ligase to the second bromodomain of BRD4 (BRD4 BD2). MMH1 binds to the JQ1-binding site of BRD4 BD2, acts as a template to covalently modify Cys58 of DCAF16, stabilizes the BRD4-DCAF16 ternary complex, and thereby promotes BRD4 degradation via the CRL4DCAF16 ubiquitin ligase pathway. Using BRD4 BD2 as a structural template, MMH1 covalently modifies Cys87 of GAK and induces the GAK-BRD4 BD2 interaction. Through its covalent mechanism, MMH1 exhibits sustained BRD4 degradation activity, and shows selective degradation activity for BRD4 BD2 over BRD4 BD1. | ||||||||||||||||||||
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Similarity Score 0.86
HY-156828MMH2 -
Similarity Score 0.84
HY-13030(+)-JQ-1 -
Similarity Score 0.84
HY-13030A(R)-(-)-JQ1 Enantiomer -
Similarity Score 0.84
HY-137075(±)-JQ1 -
Similarity Score 0.83
HY-153385TMX1 -
Similarity Score 0.81
HY-136857BRD4 degrader-3 -
Similarity Score 0.76
HY-111139MS417 -
Similarity Score 0.74
HY-116349Bromodomain IN-1 -
Similarity Score 0.74
HY-176438DDL-357 -
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