Black Diamond's MAP Platform


Black Diamond Therapeutics has developed a proprietary method to discover, uncover, and target allosteric mutant oncogenes.

Black Diamond Therapeutics is using its MAP platform to extend its approach to developing drugs to a range of high value oncogenic targets.

Screening for Potent & Selective Targeted Therapies

At Black Diamond Therapeutics we exploit protein allostery to develop selective precision medicines with favorable safety and efficacy profiles.

A New Approach to
Developing Precision Medicine

Discover, Uncover and Target



Black Diamond Therapeutics mines mutational hotspots for allosteric sites that produce potent oncogenes

Our computational platform integrates multiple forms of genome-level data with a deep understanding of mechanism, structure and dynamics.



Black Diamond's platform provides insights into how allosteric mutations drive oncogenic activation

Allosterically activated oncogenes are identified by mapping mutation onto regulatory domains and regions involved protein-protein interfaces.

Protein Pharmacology


Black Diamond Therapeutics exploits this unique pharmacology to design drugs that are potent and selective for allosteric mutant oncogenes

Allosteric oncogenes are validated through screening in proprietary models of cancer.

The Science of Black Diamond

What is an allosteric mutation?

An allosteric mutation occurs distal to the site of action of an enzyme or receptor. In receptor tyrosine kinases, allosteric mutations occur distal to the the ATP binding site. 

Because large-scale conformational changes in proteins are a prerequisite for dimerization in oncogenic RTKs, allosteric mutations most frequently occur at, and structurally alter, the dimerization interface.

How are allosteric mutations oncogenic?

Allosteric mutations activate tumor drivers and inactivate tumor suppressors through the large scale conformational change.

How are allosteric mutations oncogenic in RTKs?

Allosteric mutations render RTK oncogenes ligand-independent.

Consequences of Allosteric Oncogenic Mutations In EGFR AND HER2

For the ErbB RTK oncogenes, EGFR and HER2, the selectivity of the ATP site is altered in comparison to the wild type receptors. Even though there is no change in the primary sequence of the ATP site, allosteric mutant ErbB RTKs exhibit unique drug selectivity.

Scientific Presentations & Publications


“EGFR Oncogenes Expressed in Glioblastoma are Activated as Covalent Dimers and Paradoxically Stimulated by Erlotinib”

Click here to view: EGFR Oncogenes Expressed In Glioblastoma Are Activated As Covalent Dimers And Paradoxically Stimulated By Erlotinib

European Society of Medical Oncology (ESMO) 2019

“Oncogenic Mutations at the Dimer Interface of EGFR Lead to Formation of Covalent Homo-Dimers and Allosteric Activation of the Kinase Domain: A Mechanism Which Alters the Selectivity Profile of Oncogenic EGFR”

Click here to view: BDTX_ESMO2019_100419_final

American Association for Cancer Research (AACR) 2019

“Epidermal Growth Factor Receptor Oncogenes Expressed in Glioblastoma are Activated as Covalent Dimers and Exhibit Unique Pharmacology”

Click here to view: BDTX_AACR2019.VF